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  • 1.
    Allahverdiyeva, Yagut
    et al.
    University of Turku.
    Mamedov, Fikret
    Uppsala University.
    Holmstrom, Maija
    University of Turku.
    Nurmi, Markus
    University of Turku.
    Lundin, Björn
    Linköping University, Department of Clinical and Experimental Medicine, Cell Biology. Linköping University, Faculty of Health Sciences.
    Styring, Stenbjorn
    Uppsala University.
    Spetea Wiklund, Cornelia
    Linköping University, Department of Physics, Chemistry and Biology. Linköping University, The Institute of Technology.
    Aro, Eva-Mari
    University of Turku.
    Comparison of the electron transport properties of the psbo1 and psbo2 mutants of Arabidopsis thaliana2009In: BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS, ISSN 0005-2728, Vol. 1787, no 10, p. 1230-1237Article in journal (Refereed)
    Abstract [en]

    Genome sequence of Arabidopsis thaliana (Arabidopsis) revealed two psbO genes (At5g66570 and At3g50820) which encode two distinct PsbO isoforms: PsbO1 and PsbO2, respectively. To get insights into the function of the PsbO1 and PsbO2 isoforms in Arabidopsis we have performed systematic and comprehensive investigations of the whole photosynthetic electron transfer chain in the T-DNA insertion mutant lines, psbO1 and psbo2. The absence of the PsbO1 isoform and presence of only the PsbO2 isoform in the psbo1 mutant results in (i) malfunction of both the donor and acceptor sides of Photosystem (PS) 11 and (ii) high sensitivity of PSII centers to photodamage, thus implying the importance of the PsbO1 isoform for proper structure and function of PSII. The presence of only the PsbO2 isoform in the PSII centers has consequences not only to the function of PSII but also to the PSI/PSII ratio in thylakoids. These results in modification of the whole electron transfer chain with higher rate of cyclic electron transfer around PSI, faster induction of NPQ and a larger size of the PQ-pool compared to WT, being in line with apparently increased chlororespiration in the psbo1 mutant plants. The presence of only the PsbO1 isoform in the psbo2 mutant did not induce any significant differences in the performance of PSII under standard growth conditions as compared to WT. Nevertheless, under high light illumination, it seems that the presence of also the PsbO2 isoform becomes favourable for efficient repair of the PSII complex.

  • 2.
    Irigoyen, Sonia
    et al.
    Texas A&M University.
    Karlsson, Patrik
    University of Gothenburg.
    Kuruvilla, Jacob
    Linköping University, Department of Clinical and Experimental Medicine. Linköping University, Faculty of Health Sciences.
    Spetea Wiklund, Cornelia
    University of Gothenburg.
    Versaw, Wayne K
    Texas A&M University.
    The Sink-Specific Plastidic Phosphate Transporter PHT4;2 Influences Starch Accumulation and Leaf Size in Arabidopsis2011In: Plant Physiology, ISSN 0032-0889, E-ISSN 1532-2548, Vol. 157, no 4, p. 1765-1777Article in journal (Refereed)
    Abstract [en]

    Nonphotosynthetic plastids are important sites for the biosynthesis of starch, fatty acids, and amino acids. The uptake and subsequent use of cytosolic ATP to fuel these and other anabolic processes would lead to the accumulation of inorganic phosphate (Pi) if not balanced by a Pi export activity. However, the identity of the transporter(s) responsible for Pi export is unclear. The plastid-localized Pi transporter PHT4;2 of Arabidopsis (Arabidopsis thaliana) is expressed in multiple sink organs but is nearly restricted to roots during vegetative growth. We identified and used pht4;2 null mutants to confirm that PHT4; 2 contributes to Pi transport in isolated root plastids. Starch accumulation was limited in pht4; 2 roots, which is consistent with the inhibition of starch synthesis by excess Pi as a result of a defect in Pi export. Reduced starch accumulation in leaves and altered expression patterns for starch synthesis genes and other plastid transporter genes suggest metabolic adaptation to the defect in roots. Moreover, pht4; 2 rosettes, but not roots, were significantly larger than those of the wild type, with 40% greater leaf area and twice the biomass when plants were grown with a short (8-h) photoperiod. Increased cell proliferation accounted for the larger leaf size and biomass, as no changes were detected in mature cell size, specific leaf area, or relative photosynthetic electron transport activity. These data suggest novel signaling between roots and leaves that contributes to the regulation of leaf size.

  • 3. Kanervo, Eira
    et al.
    Spetea, Cornelia
    Linköping University, Faculty of Health Sciences. Linköping University, Department of Biomedicine and Surgery, Cell biology.
    Nishiyama, Yoshitaka
    Murata, Norio
    Andersson, Bertil
    Linköping University, Faculty of Health Sciences. Linköping University, Department of Biomedicine and Surgery, Cell biology.
    Aro, Eva-Mari
    Dissecting a cyanobacterial proteolytic system: Efficiency in inducing degradation of the D1 protein of photosystem II in cyanobacteria and plants2003In: Biochimica et Biophysica Acta - Bioenergetics, ISSN 0005-2728, E-ISSN 1879-2650, Vol. 1607, no 2-3, p. 131-140Article in journal (Refereed)
    Abstract [en]

    A chromatography fraction, prepared from isolated thylakoids of a fatty acid desaturation mutant (Fad6/desAKmr) of the cyanobacterium Synechocystis 6803, could induce an initial cleavage of the D1 protein in Photosystem II (PSII) particles of Synechocystis 6803 mutant and Synechococcus 7002 wild type as well as in supercomplexes of PSII-light harvesting complex II of spinach. Proteolysis was demonstrated both in darkness and in light as a reduction in the amount of full-length D1 protein or as a production of C-terminal initial degradation fragments. In the Synechocystis mutant, the main degradation fragment was a 10-kDa C-terminal one, indicating an initial cleavage occurring in the cytoplasmic DE-loop of the D1 protein. A protein component of 70-90 kDa isolated from the chromatographic fraction was found to be involved in the production of this 10-kDa fragment. In spinach, only traces of the corresponding fragment were detected, whereas a 24-kDa C-terminal fragment accumulated, indicating an initial cleavage in the lumenal AB-loop of the D1 protein. Also in Synechocystis the 24-kDa fragment was detected as a faint band. An antibody raised against the Arabidopsis DegP2 protease recognized a 35-kDa band in the proteolytically active chromatographic fraction, suggesting the existence of a lumenal protease that may be the homologue DegP of Synechocystis. The identity of the other protease cleaving the D1 protein in the DE-loop exposed on the stromal (cytoplasmic) side of the membrane is discussed. ⌐ 2003 Elsevier B.V. All rights reserved.

  • 4. Lindahl, Marika
    et al.
    Spetea, Cornelia
    Linköping University, Faculty of Health Sciences. Linköping University, Department of Biomedicine and Surgery, Cell biology.
    Hundal, Torill
    Linköping University, Faculty of Health Sciences. Linköping University, Department of Biomedicine and Surgery, Cell biology.
    Oppenheim, Amos
    Adam, Zach
    Andersson, Bertil
    Linköping University, Faculty of Health Sciences. Linköping University, Department of Biomedicine and Surgery, Cell biology.
    The thylakoid FtsH protease plays a role in the light-induced turnover of the photosystem II D1 protein2000In: The Plant Cell, ISSN 1040-4651, E-ISSN 1532-298X, Vol. 12, no 3, p. 419-431Article in journal (Refereed)
    Abstract [en]

    The photosystem II reaction center D1 protein is known to turn over frequently. This protein is prone to irreversible damage caused by reactive oxygen species that are formed in the light, the damaged, nonfunctional D1 protein is degraded and replaced by a new copy. However, the proteases responsible for D1 protein degradation remain unknown. In this study, we investigate the possible role of the FtsH protease, an ATP-dependent zinc metalloprotease, during this process. The primary light-induced cleavage product of the D1 protein, a 23-kD fragment, was found to be degraded in isolated thylakoids in the dark during a process dependent on ATP hydrolysis and divalent metal ions, suggesting the involvement of FtsH. Purified FtsH degraded the 23-kD D1 fragment present in isolated photosystem II core complexes, as well as that in thylakoid membranes depleted of endogenous FtsH. In this study, we definitively identify the chloroplast protease acting on the D1 protein during its light-induced turnover. Unlike previously identified membrane-bound substrates for FtsH in bacteria and mitochondria, the 23-kD D1 fragment represents a novel class of FtsH substrate - functionally assembled proteins that have undergone irreversible photooxidative damage and cleavage.

  • 5.
    Lundin, Björn
    et al.
    Linköping University, Department of Clinical and Experimental Medicine, Cell Biology. Linköping University, Faculty of Health Sciences.
    Hansson, Maria
    Linköping University, Department of Clinical and Experimental Medicine, Cell Biology. Linköping University, Faculty of Health Sciences.
    Schoefs, Benoít
    Dynamique Vacuolaire et Réponses aux Stress de l'Environnement, Université de Bourgogne, Dijon cedex, France.
    Vener, Alexander V
    Linköping University, Department of Clinical and Experimental Medicine, Cell Biology. Linköping University, Faculty of Health Sciences.
    Spetea (Wiklund), Cornelia
    Linköping University, Department of Clinical and Experimental Medicine, Cell Biology. Linköping University, Faculty of Health Sciences.
    Arabidopsis PsbO2 protein regulates dephosphorylation and turnover of the photosystem II reaction centre D1 protein2007In: The Plant Journal, ISSN 0960-7412, Vol. 49, no 3, p. 528-539Article in journal (Refereed)
    Abstract [en]

    The extrinsic photosystem II (PSII) protein of 33 kDa (PsbO), which stabilizes the water-oxidizing complex, is represented in Arabidopsis thaliana (Arabidopsis) by two isoforms. Two T-DNA insertion mutant lines deficient in either the PsbO1 or the PsbO2 protein were retarded in growth in comparison with the wild type, while differing from each other phenotypically. Both PsbO proteins were able to support the oxygen evolution activity of PSII, although PsbO2 was less efficient than PsbO1 under photoinhibitory conditions. Prolonged high light stress led to reduced growth and fitness of the mutant lacking PsbO2 as compared with the wild type and the mutant lacking PsbO1. During a short period of treatment of detached leaves or isolated thylakoids at high light levels, inactivation of PSII electron transport in the PsbO2-deficient mutant was slowed down, and the subsequent degradation of the D1 protein was totally inhibited. The steady-state levels of in vivo phosphorylation of the PSII reaction centre proteins D1 and D2 were specifically reduced in the mutant containing only PsbO2, in comparison with the mutant containing only PsbO1 or with wild-type plants. Phosphorylation of PSII proteins in vitro proceeded similarly in thylakoid membranes from both mutants and wild-type plants. However, dephosphorylation of the D1 protein occurred much faster in the thylakoids containing only PsbO2. We conclude that the function of PsbO1 in Arabidopsis is mostly in support of PSII activity, whereas the interaction of PsbO2 with PSII regulates the turnover of the D1 protein, increasing its accessibility to the phosphatases and proteases involved in its degradation.

  • 6.
    Lundin, Björn
    et al.
    Linköping University, Department of Physics, Chemistry and Biology, Molecular genetics . Linköping University, The Institute of Technology.
    Nurmi, Markus
    University of Turku.
    Rojas-Stuetz, Marc
    University of Konstanz.
    Aro, Eva-Mari
    University of Turku.
    Adamska, Iwona
    University of Konstanz.
    Spetea Wiklund , Cornelia
    Linköping University, Department of Physics, Chemistry and Biology, Molecular genetics . Linköping University, The Institute of Technology.
    Towards understanding the functional difference between the two PsbO isoforms in Arabidopsis thaliana-insights from phenotypic analyses of psbo knockout mutants2008In: Photosynthesis Research, ISSN 0166-8595, E-ISSN 1573-5079, Vol. 98, no 1-3, p. 405-414Article in journal (Refereed)
    Abstract [en]

    The extrinsic PsbO subunit of the water-oxidizing photosystem II (PSII) complex is represented by two isoforms in Arabidopsis thaliana, namely PsbO1 and PsbO2. Recent analyses of psbo1 and psbo2 knockout mutants have brought insights into their roles in photosynthesis and light stress. Here we analyzed the two psbo mutants in terms of PsbOs expression pattern, organization of PSII complexes and GTPase activity. Both PsbOs are present in wild-type plants, and their expression is mutually controlled in the mutants. Almost all PSII complexes are in the monomeric form not only in the psbo1 but also in the psbo2 mutant grown under high-light conditions. This results either from an enhanced susceptibility of PSII to photoinactivation or from malfunction of the repair cycle. Notably, the psbo1 mutant displays such problems even under growth-light conditions. These results together with the finding that PsbO2 has a threefold higher GTPase activity than PsbO1 have significance for the turnover of the PSII D1 subunit in Arabidopsis.

  • 7.
    Lundin, Björn
    et al.
    Linköping University, Department of Clinical and Experimental Medicine, Cell Biology. Linköping University, Faculty of Health Sciences.
    Thuswaldner (Heurtel), Sophie
    Linköping University, Department of Clinical and Experimental Medicine, Cell Biology. Linköping University, Faculty of Health Sciences.
    Shutova, Tatiana
    Department of Plant Physiology, Umeå Plant Science Center, Umeå University, Umeå, Sweden.
    Eshaghi, Said
    Linköping University, Department of Clinical and Experimental Medicine, Cell Biology. Linköping University, Faculty of Health Sciences.
    Samuelsson, Göran
    Department of Plant Physiology, Umeå Plant Science Center, Umeå University, Umeå, Sweden.
    Barber, Jim
    Wolfson Laboratories, Division of Molecular Biosciences, Imperial College, London, UK.
    Andersson, Bertil
    Linköping University, Department of Clinical and Experimental Medicine, Cell Biology. Linköping University, Faculty of Health Sciences.
    Spetea (Wiklund), Cornelia
    Linköping University, Department of Clinical and Experimental Medicine, Cell Biology. Linköping University, Faculty of Health Sciences.
    Subsequent events to GTP binding by the plant PsbO protein: structural changes, GTP hydrolysis and dissociation from the photosystem II complex2007In: Biochimica et Biophysica Acta - Bioenergetics, ISSN 0005-2728, E-ISSN 1879-2650, Vol. 1767, no 6, p. 500-508Article in journal (Refereed)
    Abstract [en]

    Besides an essential role in optimizing water oxidation in photosystem II (PSII), it has been reported that the spinach PsbO protein binds GTP [C. Spetea, T. Hundal, B. Lundin, M. Heddad, I. Adamska, B. Andersson, Proc. Natl. Acad. Sci. U.S.A. 101 (2004) 1409–1414]. Here we predict four GTP-binding domains in the structure of spinach PsbO, all localized in the β-barrel domain of the protein, as judged from comparison with the 3D-structure of the cyanobacterial counterpart. These domains are not conserved in the sequences of the cyanobacterial or green algae PsbO proteins. MgGTP induces specific changes in the structure of the PsbO protein in solution, as detected by circular dichroism and intrinsic fluorescence spectroscopy. Spinach PsbO has a low intrinsic GTPase activity, which is enhanced fifteen-fold when the protein is associated with the PSII complex in its dimeric form. GTP stimulates the dissociation of PsbO from PSII under light conditions known to also release Mn2+ and Ca2+ ions from the oxygen-evolving complex and to induce degradation of the PSII reaction centre D1 protein. We propose the occurrence in higher plants of a PsbO-mediated GTPase activity associated with PSII, which has consequences for the function of the oxygen-evolving complex and D1 protein turnover.

  • 8.
    Lundin, Björn
    et al.
    Linköping University, Department of Clinical and Experimental Medicine, Cell Biology. Linköping University, Faculty of Health Sciences.
    Thuswaldner (Heurtel), Sophie
    Linköping University, Department of Clinical and Experimental Medicine, Cell Biology. Linköping University, Faculty of Health Sciences.
    Spetea (Wiklund), Cornelia
    Linköping University, Department of Clinical and Experimental Medicine, Cell Biology. Linköping University, Faculty of Health Sciences.
    Arabidopsis PsbOs differ in their GTPase activity2008In: Photosynthesis: Energy from the Sun / [ed] John F. Allen, Elisabeth Gantt, John H. Golbeck, Barry Osmond., Springer , 2008, p. 729-731Chapter in book (Other academic)
    Abstract [en]

    Crucial for the optimal function of the oxygen-evolving complex (OEC) is the PsbO subunit of the photosystem II (PSII) complex. Previously we reported the ability of PsbO in spinach to bind and hydrolyze GTP. GTP stimulates the dissociation of PsbO from PSII following illumination and induces the degradation of the D1 protein. We have predicted four plant-specific binding motifs for GTP, which are not conserved in the sequences of the cyanobacteria or green algae PsbO proteins. We have proposed a location of the GTP-binding site inside the β-barrel exposed to the lumenal side. Arabidopsis thaliana has two PsbO isoforms encoded by two different genes: psbO1 and psbO2. Here we have measured and compared the GTPase activities of PSII membranes isolated from Arabidopsis knockouts mutants containing T-DNA insertions in one or the other of the psbO genes. The specific GTPase activity of PsbO2 is three fold higher than that of PsbO1. Furthermore, PsbO2 is more efficiently released than PsbO1 from PSII following light treatment. We conclude that PsbO2 is a better GTPase than Psb.

  • 9.
    Ruiz Pavón, Lorena
    et al.
    Linköping University, Department of Physics, Chemistry and Biology, Molecular genetics . Linköping University, The Institute of Technology.
    Karlsson, Patrik
    Linköping University, Department of Physics, Chemistry and Biology, Molecular genetics . Linköping University, The Institute of Technology.
    Carlsson, Jonas
    Linköping University, Department of Physics, Chemistry and Biology, Bioinformatics . Linköping University, The Institute of Technology.
    Samyn, Dieter
    School of Pure and Applied Natural Sciences, Kalmar University, 391 82 Kalmar, Sweden.
    Persson, Bengt
    Linköping University, Department of Physics, Chemistry and Biology, Bioinformatics . Linköping University, The Institute of Technology.
    Persson, Bengt L.
    School of Pure and Applied Natural Sciences, Kalmar University, 391 82 Kalmar, Sweden.
    Spetea, Cornelia
    Linköping University, Department of Physics, Chemistry and Biology, Molecular genetics . Linköping University, The Institute of Technology.
    Functionally Important Amino Acids in the Arabidopsis Thylakoid Phosphate Transporter: Homology Modeling and Site-directed Mutagenesis2010In: Biochemistry, ISSN 0006-2960, E-ISSN 1520-4995, Vol. 49, no 30, p. 6430-6439Article in journal (Other academic)
    Abstract [en]

    The anion transporter 1 (ANTR1) from Arabidopsis thaliana, homologous to the mammalian SLC17 family, has recently been localized to the chloroplast thylakoid membrane. When expressed heterologously in Escherichia coli, ANTR1 mediates a Na+-dependent active transport of inorganic phosphate (Pi). The aim of this study was to identify amino acids involved in substrate binding/translocation by ANTR1 and in the Na+-dependence of its activity. A threedimensional structural model of ANTR1 was constructed using the crystal structure of glycerol-3-phosphate/phosphate antiporter (GlpT) from E.coli as a template. Based on this model and multiple sequence alignments, five highly conserved residues in plant ANTRs and mammalian SLC17 homologues have been selected for site-directed mutagenesis, namely Arg-120, Ser-124 and Arg-201 inside the putative translocation pathway, Arg-228 and Asp-382 exposed at the cytosolic surface of the protein. The activities of the wild type and mutant proteins have been analyzed using expression in E. coli and radioactive transport assays, and compared with bacterial cells carrying an empty plasmid. Based on Pi- and Na+-dependent kinetics, we propose that Arg-120, Arg-201 and Arg-228 are involved in binding and translocation of the substrate, Ser-124 functions as a periplasmic gate for Na+ ions, and finally Asp-382 participates in the turnover of the transporter via ionic interaction with either Arg-228 or Na+ ions. We also propose that the corresponding residues may have a similar function in other plant and mammalian SLC17 homologous transporters.

  • 10.
    Ruiz Pavón, Lorena
    et al.
    Linköping University, Department of Physics, Chemistry and Biology, Molecular genetics . Linköping University, The Institute of Technology.
    Lundh, Fredrik
    School of Pure and Applied Natural Sciences, Kalmar University, Kalmar, Sweden .
    Lundin, Björn
    Linköping University, Department of Physics, Chemistry and Biology, Molecular genetics . Linköping University, The Institute of Technology.
    Mishra, Arti
    Linköping University, Department of Physics, Chemistry and Biology, Molecular genetics . Linköping University, The Institute of Technology.
    Persson, Bengt
    School of Pure and Applied Natural Sciences, Kalmar University, Kalmar, Sweden.
    Spetea (Wiklund), Cornelia
    Linköping University, Department of Physics, Chemistry and Biology, Molecular genetics . Linköping University, The Institute of Technology.
    Arabidopsis ANTR1 is a thylakoid Na+-dependent phosphate transporter -functional characterization in Escherichia coli2008In: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 283, no 20, p. 13520-13527Article in journal (Refereed)
    Abstract [en]

    In this study, the putative anion transporter 1 (ANTR1) from Arabidopsis thaliana was shown to be localized to the chloroplast thylakoid membrane by Western blotting with two different peptide-specific antibodies. ANTR1 is homologous to the type I of mammalian Na+-dependent inorganic phosphate (Pi) transporters. The function of ANTR1 as a Na+-dependent Pi transporter was demonstrated by heterologous expression and uptake of radioactive Pi into Escherichia coli cells. The expression of ANTR1 conferred increased growth rates to the transformed cells and stimulated Pi uptake in a pH- and Na+-dependent manner as compared with the control cells. Among various tested effectors, Pi was the preferred substrate. Although it competed with the uptake of Pi, glutamate was not transported by ANTR1 into E. coli. In relation to its function as a Pi transporter, several physiological roles for ANTR1 in the thylakoid membrane are proposed, such as export of Pi produced during nucleotide metabolism in the thylakoid lumen back to the chloroplast stroma and balance of the trans-thylakoid H+ electrochemical gradient storage.

  • 11. Ruiz Pavón, Lorena
    et al.
    Mishra, A.
    Lundh, F.
    Persson, B.
    Spetea Wiklund, Cornelia
    Linköping University, Faculty of Health Sciences.
    Localization and functional studies of Arabidopsis anion transporter 12008In: Photosynthesis 2007: Energy from the Sun,2007, Springer Publisher , 2008, p. 1063-1066Conference paper (Other academic)
  • 12.
    Ruiz-Pavon, L
    et al.
    Linnaeus University, School of Natural Sciences, Kalmar, Sweden,.
    Karlsson, Patrik
    Linköping University, Department of Physics, Chemistry and Biology, Molecular genetics. Linköping University, The Institute of Technology.
    Carlsson, Jonas
    Linköping University, Department of Physics, Chemistry and Biology, Bioinformatics. Linköping University, The Institute of Technology.
    Samyn, D
    Linnaeus University, School of Natural Sciences, Kalmar, Sweden,.
    Persson, Bengt
    Linköping University, Department of Physics, Chemistry and Biology, Bioinformatics. Linköping University, The Institute of Technology.
    Persson, B L
    Linnaeus University, School of Natural Sciences, Kalmar, Sweden,.
    Spetea Wiklund, Cornelia
    Linköping University, Department of Physics, Chemistry and Biology, Molecular genetics. Linköping University, The Institute of Technology.
    Modeling and Mutational analysis of Anion transporter 1 protein of Arabidopsis thaliana2010In: The FEBS Journal, ISSN 1742-464X, E-ISSN 1742-4658, Vol. 277, no Suppl. 1, p. 231-231Article in journal (Other academic)
    Abstract [en]

    The  thylakoid   anion  transporter 1  (ANTR1)   from  Arabidopsisthaliana,  has been characterized as a Na-dependent Pi transporter when expressed in E. coli (1), but  no data  is yet available  for the protein  structure  and  amino  acids involved in transport of Pi. In this  study  a  three-dimensional structural  model  of  ANTR1  was constructed in silico using the crystal structure  of glycerol-3- phosphate/phosphate antiporter from E. coli as a template.  Based on Multiple  Sequence Alignments (MSAs) with other plant  ANT- Rs  and  mammalian   SLC17  homologues,   five  highly  conserved amino  acids involved in Pi transport have been identified,  namely Arg-120, Ser-124 and Arg-201 inside the putative translocation pathway,  Arg-228  and  Asp-382  exposed  at  the  cytoplasmic  sur- face of the protein.  The activity of the protein  as a Na-dependent Pi transporter in the wild type and mutants  was analyzed  by het- erologous  expression  and  uptake   of  radioactive   Pi  into  E.  coli cells. Substitution of the three Arg (120, 201 and 228) for Glu residues  and  of Asp-382 for  an  Asn residue  resulted  in an  inac- tive ANTR1  transporter. All other  mutants  had sufficient activity to  allow  measurement   of  kinetic  parameters, attesting   that  the mutated  proteins  were functional.  Based on  our  results,  we pro- pose that Arg-201 is a critical residue for substrate  binding and translocation, whereas Ser-124 may function  as periplasmic  gate- way for  Na+   ions.  Residue  Arg-120  plays  an  important role  in Pi  binding  and  associated   conformational  changes,  and  finally that Arg-228 and Asp-382 only weakly participate  in interactions allowing conformational changes to occur at the cytoplasmic  sur-face of the transporter.

  • 13.
    Spetea, Cornelia
    et al.
    Linköping University, Faculty of Health Sciences. Linköping University, Department of Biomedicine and Surgery, Cell biology.
    Keren, Nir
    Hundal, Torill
    Linköping University, Faculty of Health Sciences. Linköping University, Department of Biomedicine and Surgery, Cell biology.
    Doan, Jean-Michel
    Ohad, Itzhak
    Andersson, Bertil
    Linköping University, Faculty of Health Sciences. Linköping University, Department of Biomedicine and Surgery, Cell biology.
    GTP enhances the degradation of the photosystem II D1 protein irrespective of its conformational heterogeneity at the Q(B) site2000In: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 275, no 10, p. 7205-7211Article in journal (Refereed)
    Abstract [en]

    The light exposure history and/or binding of different herbicides at the Q(B) site may induce heterogeneity of photosystem II acceptor side conformation that affects D1 protein degradation under photoinhibitory conditions. GTP was recently found to stimulate the D1 protein degradation of photoinactivated photosystem II (Spetea C., Hundal, T., Lohmann, F., and Andersson, B. (1999) Proc. Natl. Acad. Sci. U. S. A. 96, 6547-6552). Here we report that GTP enhances the cleavage of the D1 protein D-E loop following exposure of thylakoid membranes to either high light, low light, or repetitive single turnover flashes but not to trypsin. GTP does not stimulate D1 protein degradation in the presence of herbicides known to affect the accessibility of the cleavage site to proteolysis. However, GTP stimulates degradation that can be induced even in darkness in some photosystem II conformers following binding of the PNO8 herbicide (Nakajima, Y., Yoshida, S., Inoue, Y., Yoneyama, K., and Ono, T. (1995) Biochim. Biophys. Acta 1230, 38-44). Both the PNO8- and the light-induced primary cleavage of the D1 protein occur in the grana membrane domains. The subsequent migration of photo-system II containing the D1 protein fragments to the stroma domains for secondary proteolysis is light-activated. We conclude that the GTP effect is not confined to a specific photoinactivation pathway nor to the conformational state of the photosystem II acceptor side. Consequently, GTP does not interact with the site of D1 protein cleavage but rather enhances the activity of the endogenous proteolytic system.

  • 14.
    Spetea, Cornelia
    et al.
    Linköping University, Department of Physics, Chemistry and Biology, Molecular genetics. Linköping University, Department of Clinical and Experimental Medicine. Linköping University, The Institute of Technology.
    Schoefs, B.
    Photosynthesis and Light Stress in a Model Plant ­Role of Chloroplast Transporters2010In: Handbook of Plant and CropStress, Third Edition / [ed] Pessarakli M., USA: CRC Press , 2010, 3, p. 361-389Chapter in book (Other academic)
    Abstract [en]

    The dynamic and expanding knowledge of environmental stresses and their effects on plants and crops have resulted in the compilation of a large volume of information in the last ten years since the publication of the second edition of the Handbook of Plant and Crop Stress. With 90 percent new material and a new organization that reflects this increased knowledge base, this new edition, like the first two, provides comprehensive and complete coverage of the issues on stress imposed on plants and crops.

    Accessibility of knowledge is among the most critical of factors involved with plant/crop stress problems. Without due consideration of all the factors contributing to a specific plant/crop stress problem, it is unlikely that a permanent solution can be found. Facilitating the accessibility of the desired information, the volume is divided into ten sections. Each section consists of one or more chapters that discuss as many aspects of stress as possible.

    While many references cover soil salinity, sodicity, specific plant/crop salt and water stress, pollution, and other environmental stresses, they exist relatively in isolation, focusing mainly on one specific topic. Prepared with input from more than a hundred contributors from twenty seven countries, this book combines information on these interrelated areas into a single resource. Packed with illustrations, figures, and tables, covering plant/crop stress problems from the soil to the atmosphere, this book puts this expanded environmental stressors knowledge base within easy reach.

  • 15.
    Spetea Wiklund, Cornelia
    et al.
    Linköping University, Department of Clinical and Experimental Medicine, Cell Biology. Linköping University, Faculty of Health Sciences.
    Hundal, Torill
    Linköping University, Department of Biomedicine and Surgery.
    Lundin, Björn
    Linköping University, Department of Clinical and Experimental Medicine, Cell Biology. Linköping University, Faculty of Health Sciences.
    Heddad, Mounia
    Department of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden.
    Adamska, Iwona
    Department of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden.
    Andersson, Bertil
    Department of Biochemistry and Biophysics, Stockholm University, Stockholm, Sweden.
    Multiple evidence for nucleotide metabolism in the chloroplast thylakoid lumen2004In: Proceedings of the National Academy of Science, ISSN 0027-8424, Vol. 101, no 5, p. 1409-1414Article in journal (Refereed)
    Abstract [en]

    The apparatus of photosynthetic energy conversion in chloroplasts is quite well characterized with respect to structure and function. Light-driven electron transport in the thylakoid membrane is coupled to synthesis of ATP, used to drive energy-dependent metabolic processes in the stroma and the outer surface of the thylakoid membrane. The role of the inner (luminal) compartment of the thylakoids has, however, remained largely unknown although recent proteomic analyses have revealed the presence of up to 80 different proteins. Further, there are no reports concerning the presence of nucleotides in the thylakoid lumen. Here, we bring three lines of experimental evidence for nucleotide-dependent processes in this chloroplast compartment. (i) The thylakoid lumen contains a protein of 17.2 kDa, catalyzing the transfer of the γ-phosphate group from ATP to GDP, proposed to correspond to the nucleoside diphosphate kinase III. (ii) The 33-kDa subunit of photosystem II, bound to the luminal side of the thylakoid membrane and associated with the water-splitting process, can bind GTP. (iii) The thylakoid membrane contains a nucleotide transport system that is suggested to be associated with a 36.5-kDa nucleotide-binding protein. Our results imply, against current dogmas, that the thylakoid lumen contains nucleotides, thereby providing unexpected aspects on this chloroplast compartment from a metabolic and regulatory perspective and expanding its functional significance beyond a pure bioenergetic function.

  • 16.
    Spetea Wiklund, Cornelia
    et al.
    Linköping University, Faculty of Health Sciences.
    Ruiz Pavón, Lorena
    Thuswaldner, S.
    Lundin, Björn
    Linköping University, Faculty of Health Sciences.
    Lundh, F.
    Persson, B.
    Schoefs, B.
    Adamska, I.
    Screening for solute transporters in plant photosynthetic membranes2008In: Photosynthesis 2007: Energy from the sun,2007, Springer Publisher , 2008, p. 1067-1070Conference paper (Other academic)
  • 17.
    Spetea Wiklund, Cornelia
    et al.
    Linköping University, Department of Physics, Chemistry and Biology, Molecular genetics. Linköping University, Faculty of Health Sciences.
    Schoefs, B.
    UMR CNRS/INRA/Université de Bourgogne - Plante Microbe Environnement; CMSE; Dijon, France.
    Solute transporters in plant thylakoid membranes­ key players during photosynthesis and light stress2010In: Communicative & Integrative Biology, ISSN 1942-0889, E-ISSN 1942-0889, Vol. 3, no 2, p. 122-129Article in journal (Refereed)
    Abstract [en]

    Plants utilize sunlight to drive photosynthetic energy conversion in the chloroplast thylakoid membrane. Here are located four major photosynthetic complexes, about which we have great knowledge in terms of structure and function. However, much less we know about auxiliary proteins, such as transporters, ensuring an optimum function and turnover of these complexes. The most prominent thylakoid transporter is the proton-translocating ATP-synthase. Recently, four additional transporters have been identified in the thylakoid membrane of Arabidopsis thaliana, namely one copper-transporting P-ATPase, one chloride channel, one phosphate transporter, and one ATP/ADP carrier. Here, we review the current knowledge on the function and physiological role of these transporters during photosynthesis and light stress in plants. Subsequently, we make a survey on the outlook of thylakoid activities awaiting identification of responsible proteins. Such knowledge is necessary to understand the thylakoid network of transporters, and to design strategies for bioengineering crop plants in the future.

  • 18.
    Spetea Wiklund, Cornelia
    et al.
    Linköping University, Department of Clinical and Experimental Medicine, Cell Biology. Linköping University, Faculty of Health Sciences.
    Thuswaldner Heurtel, Sophie
    Linköping University, Department of Clinical and Experimental Medicine, Cell Biology. Linköping University, Faculty of Health Sciences.
    Update in nucleotide-dependent processes in plant chloroplasts2008In: Current Knowledge in Plant Cell Compartments / [ed] Spetea, C.Thuswaldner, S., Kerala: Research Signpost Publisher , 2008, p. 105-149Chapter in book (Other academic)
    Abstract [en]

    Chloroplasts are photosynthetically active plastids found in all green plant cells. They have two types of membranes, the double envelope membrane surrounding the organelle and the thylakoid membrane containing the photosynthetic machinery. The envelope membrane represents the interface between the cytosol and chloroplast stroma, whereas the thylakoid membrane is the interface between the stroma and the lumenal space. This chapter attempts to give an update in nucleotide-dependent processes in plant chloroplasts. The current knowledge is that ATP is produced in the light-dependent photosynthetic reactions in the thylakoid membrane, and is used during CO2-fixation in the stroma as well as in the energy-dependent processes occurring on the thylakoid and envelope membranes. There is also increasing evidence that the thylakoid lumen is a chloroplast compartment with an unexpectedly active nucleotide metabolism, expanding its function beyond a bioenergetic perspective. Here we will discuss three distinct classes of chloroplast nucleotide-binding proteins: (i) transporters involved in ATP synthesis, translocation and utilization; (ii) nucleoside diphosphate kinases, involved in conversion of ATP to other nucleotides; and (iii) GTP-binding proteins, using the energy of GTP hydrolysis to drive various processes during chloroplast biogenesis, function and turnover. The main aspects reviewed for each chloroplast protein will be prediction, proteomic and/or individual identification, in vitro biochemical characterization and in planta functional analysis.

  • 19.
    Spetea Wiklund, Cornelia
    et al.
    Linköping University, The Institute of Technology. Linköping University, Department of Physics, Chemistry and Biology, Molecular genetics. Linköping University, Department of Clinical and Experimental Medicine. Linköping University, Department of Biomedicine and Surgery, Division of cell biology.
    Thuswaldner, Sophie
    Update in nucleotide-dependent processes in plant chloroplasts2008In: Plant Cell Compartments - Selected Topics / [ed] Benoît Schoefs, Kerala, India: Research Signpost , 2008, p. 104-149Chapter in book (Other academic)
    Abstract [en]

       Membranes separate the interior medium from the exterior. Obviously, separation does not mean isolation and the membranes, as we can see them at present, act as selective filters across which different types of compounds such as salts, waste, nutriments, nucleotides, etc are transported. Depending on the molecule to be transported several ways can be used. How nucleotides are transported through the thylakoid membranes to the lumen and used in the chloroplast is the aim of the chapter by Drs. Spetea and Thuswaldner, while that of Drs. Paulilo and Falkenkrog reviews the composition of nuclear pores that mediate all the traffic between the nucleus and cytoplasm. In which ways, during evolution, the first cells were formed and how the different compartments appeared remain as tremendously exciting questions, but so far unsolved in many cases. Several theories have been proposed.

    The best known is that proposed by Margulis (1970), according to which an ancestral anaerobic prokaryote would become able to ingest solid particles such as other prokaryotes. In some cases the ingested bacteria continued to live and have evolved to give different types of membranes that eukaryotic cells contain today. This theory, also called the endosymbiotic theory, explains the origin of both the chloroplasts and the mitochondria, two major organelles of plant cells. More recently, another symbiotic theory has been proposed by Martin and Müller (1998) to explain the origin of mitochondria. While the contribution by Dr. Bizanz and collaborators traces back the unexpected fate of plastids in today's prokaryotic parasites of animal cells, the chapters by Drs. Solymosi and Schoefs, Dr. Chamarovsky and collaborators and, Dr. Rohacek and collaborators are dedicated to the biogenesis and functioning of the chloroplast membranes. The way of differentiation of the other organelles and cell compartments remain so far as unanswered questions. The search for analoguous compartments in lower organisms may provide the first elements of an answer.

    the chapter by Dr. H. Guo enters in this frame and offers a good example for the existence of a putative, so far unrevealed compartment analogue to the higher plant vacuole in cyanobacteria. The plant cell turgor is maintained thanks to the functioning of two typical compartments of plant cells i.e. the cell-wall and the vacuole, but these compartments play other important roles in plant physiology. The chapters by Dr. El Gharras and Dr. Martinez on the accumulation of betalain pigments in vacuoles and strawberry cell-wall softening, respectively, illustrate these aspects of the field. Even if plant cells are surrounded by a thick and rigid cell-wall, their interior is highly dynamic: the organelles are able to move. The contribution by Dr. Foissner analyzes the dynamic of mitochondria in Chara internodal cells. In contrast to animals, plants cannot escape from adverse conditions. Consequently, they have developed strategies to survive to biotic or/and abiotic stresses.

    In this book the description of the answers of plants to several stresses are the aim of some chapters. While the contribution by Dr. Ben Khaled and collaborators reports on the peroxidase activity in palm plantlets inoculated with arbuscular mycorrhiza fungi in the presence of biocontrol agents, the chapter by Dr. Dumas-Gaudot and collaborators, describes the modifications in the protein composition occuring during the differentiation of the arbuscules. The formation of the arbuscule is accompanied by a redistribution of the colonized root cell organelles around the arbuscule and by a dramatic change in the plastid metabolism allowing them to produce secondary metabolites, including secondary carotenoid and apocarotenoid molecules (chapter by Dr. Fester). Abiotic stresses, such as nitrogen deficiency, are also able to trigger the production of secondary carotenoids. Dr. Lemoine and collaborators review such a strategy in green algae. Because secondary carotenoids are usually high added value compounds, the knowledge about the functioning of the different compartments in such a production is also of great importance for the economic side of plant science s.l.

    How chloroplasts cope with heavy metals is discussed in the chapter by Dr. Poirier and collaborators. During the last years, new technical tools such as confocal imaging became more popular. Their use revealed the presence of new compartments, sometimes being divided into subtle sub-compartments. The intention of this book is to bring together a serie of outstanding contributions dealing with the biosynthesis, content, distribution, function, and physiology of various plant cell compartments. By combining the major contributions in this book, I wished to contribute to the propagation of the recent developments in plant cell biochemistry and physiology, to the discovery of the wonderful plant world and, also, to mutual exchange of ideas. Without the excellent work of the different authors, who have taken great care to present an up-to-date review of their field and 'Research Signpost' as the commercial editor, this book could not have been produced. I wish to dedicate this book to the different mentors in Belgium, Czech Republic and France, who showed me the scientific way and, also to my wife for her everlasting support to me.

  • 20.
    Thuswaldner (Heurtel), Sophie
    et al.
    Linköping University, Department of Biomedicine and Surgery. Linköping University, Faculty of Health Sciences.
    Rojas-Stütz, Marc
    Der, Christophe
    Leborgne-Castel, Nathalie
    Mishra, Arti
    Marty, Francis
    Schoefs, Benoît
    Adamska, Iwona
    Persson, Bengt L.
    Spetea (Wiklund), Cornelia
    Lagerstedt, Jens O.
    Bouhidel, Karim
    Identification of an ATP/ADP carrier in the Arabidopsis chloroplast thylakoid membrane. Heterologous expression and functional characterization.2006Article in journal (Refereed)
  • 21.
    Thuswaldner, Sophie
    et al.
    Linköping University, Faculty of Health Sciences. Linköping University, Department of Biomedicine and Surgery, Division of cell biology.
    Lagerstedt, Jens O
    Rojas-Stütz, Marc
    Bouhidel, Karim
    Der, Christophe
    Leborgne-Castel, Nathalie
    Mishra, Arti
    Marty, Francis
    Schoefs, Benoit
    Adamska, Iwona
    Persson, Bengt L
    Spetea Wiklund, Cornelia
    Linköping University, Faculty of Health Sciences. Linköping University, Department of Biomedicine and Surgery, Division of cell biology.
    Identification, expression, and functional analyses of a thylakoid ATP/ADP carrier from Arabidopsis2007In: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 282, no 12, p. 8848-8859Article in journal (Refereed)
    Abstract [en]

    In plants the chloroplast thylakoid membrane is the site of light-dependent photosynthetic reactions coupled to ATP synthesis. The ability of the plant cell to build and alter this membrane system is essential for efficient photosynthesis. A nucleotide translocator homologous to the bovine mitochondrial ADP/ATP carrier (AAC) was previously found in spinach thylakoids. Here we have identified and characterized a thylakoid ATP/ADP carrier (TAAC) from Arabidopsis. (i) Sequence homology with the bovine AAC and the prediction of chloroplast transit peptides indicated a putative carrier encoded by the At5g01500 gene, as a TAAC. (ii) Transiently expressed TAAC-green fluorescent protein fusion construct was targeted to the chloroplast. Western blotting using a peptide-specific antibody together with immunogold electron microscopy revealed a major location of TAAC in the thylakoid membrane. Previous proteomic analyses identified this protein in chloroplast envelope preparations. (iii) Recombinant TAAC protein specifically imports ATP in exchange for ADP across the cytoplasmic membrane of Escherichia coli. Studies on isolated thylakoids from Arabidopsis confirmed these observations. (iv) The lack of TAAC in an Arabidopsis T-DNA insertion mutant caused a 30-40% reduction in the thylakoid ATP transport and metabolism. (v) TAAC is readily expressed in dark-grown Arabidopsis seedlings, and its level remains stable throughout the greening process. Its expression is highest in developing green tissues and in leaves undergoing senescence or abiotic stress. We propose that the TAAC protein supplies ATP for energy-dependent reactions during thylakoid biogenesis and turnover in plants. © 2007 by The American Society for Biochemistry and Molecular Biology, Inc.

  • 22.
    Yin, Lan
    et al.
    Linköping University, Department of Physics, Chemistry and Biology, Molecular genetics. Linköping University, The Institute of Technology.
    Karlsson, Patrik
    Linköping University, Department of Physics, Chemistry and Biology, Molecular genetics. Linköping University, The Institute of Technology.
    Spetea Wiklund, Cornelia
    Linköping University, Department of Physics, Chemistry and Biology, Molecular genetics. Linköping University, The Institute of Technology.
    Aro, E-M
    University of Turku, Turku, Finland.
    Schoefs, B
    Université de Bourgogne, Dijon, France.
    Chloroplast thylakoid transporters2010In: The FEBS Journal, ISSN 1742-464X, E-ISSN 1742-4658, Vol. 277, no Suppl. 1, p. 231-231Article in journal (Other academic)
    Abstract [en]

    The aim of this study is to identify and functionally characterizesolute transporters from the chloroplast thylakoid membrane ofArabidopsis thaliana. As compared to chloroplast envelope transporters,much less information is available for transport processesacross the thylakoid membrane, which is mostly studied as thesite of light-driven photosynthetic reactions coupled to ATP synthesis.Although there are many reported examples of transportactivities, only a few thylakoid transporters have been identifiedat the gene level. Using bioinformatics analyses, we have predictedthe existence of approx. fifteen thylakoid transporters. Forexperimental validation, we have carried out immuno-localizationstudies used peptide-specific antibodies, functional analyses inheterologous system and validation using knockout mutants. Wehave recently identified one ATP/ADP carrier (Thuswaldneret al. JBC 2007) and one Na(+)-dependent phosphate transporter(Ruiz Pavon et al. JBC 2008). They are proposed to participatein the nucleotide metabolism in the thylakoid lumen(Spetea et al. PNAS 20004) as well as to balance the transthylakodproton electrochemical gradient storage. Based on phenotypicanalyses of knockout mutants, we will present novel dataabout the key physiological role of the two transporters duringthe high-light-induced repair of photosystem II complex in thethylakoid membrane. Subsequently, we will make a survey on theoutlook of thylakoid activities awaiting identification of responsibleproteins. Such knowledge is necessary to understand the thylakoidnetwork of transporters, and its role in photosynthesisand adaptation to environmental stress.

  • 23.
    Yin, Lan
    et al.
    Linköping University, Department of Physics, Chemistry and Biology. Linköping University, The Institute of Technology.
    Lundin, Björn
    Linköping University, Department of Clinical and Experimental Medicine, Cell Biology. Linköping University, The Institute of Technology.
    Bertrand, Martine
    National Institute for Marine Science and Technology, France .
    Nurmi, Markus
    University of Turku.
    Solymosi, Katalin
    Eotvos Lorand University.
    Kangasjarvi, Saijaliisa
    University of Turku.
    Aro, Eva-Mari
    University of Turku.
    Schoefs, Benoit
    University of Bourgogne.
    Spetea Wiklund, Cornelia
    Linköping University, Department of Biomedicine and Surgery, Division of cell biology. Linköping University, The Institute of Technology.
    Role of Thylakoid ATP/ADP Carrier in Photoinhibition and Photoprotection of Photosystem II in Arabidopsis2010In: PLANT PHYSIOLOGY, ISSN 0032-0889, Vol. 153, no 2, p. 666-677Article in journal (Refereed)
    Abstract [en]

    The chloroplast thylakoid ATP/ADP carrier (TAAC) belongs to the mitochondrial carrier superfamily and supplies the thylakoid lumen with stromal ATP in exchange for ADP. Here, we investigate the physiological consequences of TAAC depletion in Arabidopsis (Arabidopsis thaliana). We show that the deficiency of TAAC in two T-DNA insertion lines does not modify the chloroplast ultrastructure, the relative amounts of photosynthetic proteins, the pigment composition, and the photosynthetic activity. Under growth light conditions, the mutants initially displayed similar shoot weight, but lower when reaching full development, and were less tolerant to high light conditions in comparison with the wild type. These observations prompted us to study in more detail the effects of TAAC depletion on photoinhibition and photoprotection of the photosystem II (PSII) complex. The steady-state phosphorylation levels of PSII proteins were not affected, but the degradation of the reaction center II D1 protein was blocked, and decreased amounts of CP43-less PSII monomers were detected in the mutants. Besides this, the mutant leaves displayed a transiently higher nonphotochemical quenching of chlorophyll fluorescence than the wild-type leaves, especially at low light. This may be attributed to the accumulation in the absence of TAAC of a higher electrochemical H+ gradient in the first minutes of illumination, which more efficiently activates photoprotective xanthophyll cycle-dependent and independent mechanisms. Based on these results, we propose that TAAC plays a critical role in the disassembly steps during PSII repair and in addition may balance the trans-thylakoid electrochemical H+ gradient storage.

1 - 23 of 23
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