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  • 1.
    Carlberg, Inger
    et al.
    Department of Biochemistry and Biophysics, Arrhenius Laboratories of Natural Sciences, Stockholm University.
    Hansson, Maria
    Linköping University, Department of Clinical and Experimental Medicine, Cell Biology. Linköping University, Faculty of Health Sciences.
    Kieselbach, Thomas
    Department of Medical Nutrition and Biosciences, Karolinska Institute, Huddinge, Sweden.
    Schröder, Wolfgang P.
    Department of Biochemistry, Umeå University, Umeå, Sweden .
    Andersson, Bertil
    Linköping University, Department of Clinical and Experimental Medicine, Cell Biology. Linköping University, Faculty of Health Sciences.
    Vener, Alexander V.
    Linköping University, Department of Clinical and Experimental Medicine, Cell Biology. Linköping University, Faculty of Health Sciences.
    A novel plant protein undergoing light-induced phosphorylation and release from the photosynthetic thylakoid membranes2003In: Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, E-ISSN 1091-6490, Vol. 100, no 2, p. 757-762Article in journal (Refereed)
    Abstract [en]

    The characteristics of a phosphoprotein with a relative electrophoretic mobility of 12 kDa have been unknown during two decades of studies on redox-dependent protein phosphorylation in plant photosynthetic membranes. Digestion of this protein from spinach thylakoid membranes with trypsin and subsequent tandem nanospray-quadrupole-time-of-flight mass spectrometry of the peptides revealed a protein sequence that did not correspond to any previously known protein. Sequencing of the corresponding cDNA uncovered a gene for a precursor protein with a transit peptide followed by a strongly basic mature protein with a molecular mass of 8,640 Da. Genes encoding homologous proteins were found on chromosome 3 of Arabidopsis and rice as well as in ESTs from 20 different plant species, but not from any other organisms. The protein can be released from the membrane with high salt and is also partially released in response to light-induced phosphorylation of thylakoids, in contrast to all other known thylakoid phosphoproteins, which are integral to the membrane. On the basis of its properties, this plant-specific protein is named thylakoid soluble phosphoprotein of 9 kDa (TSP9). Mass spectrometric analyses revealed the existence of non-, mono-, di-, and triphosphorylated forms of TSP9 and phosphorylation of three distinct threonine residues in the central part of the protein. The phosphorylation and release of TSP9 from the photosynthetic membrane on illumination favor participation of this basic protein in cell signaling and regulation of plant gene expression in response to changing light conditions.

  • 2.
    Edvardsson, Anna
    et al.
    Linköping University, Department of Clinical and Experimental Medicine, Cell Biology. Linköping University, Faculty of Health Sciences.
    Eshaghi, Said
    Department of Biochemistry and Biophysics, Arrhenius Laboratories for Natural Sciences, Stockholm University, Stockholm, Sweden.
    Vener, Alexander V.
    Department of Biochemistry and Biophysics, Arrhenius Laboratories for Natural Sciences, Stockholm University, Stockholm, Sweden.
    Andersson, Bertil
    Department of Biochemistry and Biophysics, Arrhenius Laboratories for Natural Sciences, Stockholm University, Stockholm, Sweden.
    The major peptidyl-prolyl isomerase activity in thylakoid lumen of plant chloroplasts belongs to a novel cyclophilin TLP202003In: FEBS Letters, ISSN 0014-5793, Vol. 542, no 1-3, p. 137-141Article in journal (Refereed)
    Abstract [en]

    Fractionation of proteins from the thylakoid lumen of spinach chloroplasts combined with peptidyl-prolyl cis/trans isomerase (PPIase) measurements revealed a major isomerase activity that was ascribed to a novel enzyme TLP20 ( hylakoid umen PIase of kDa). TLP20 was inhibited by cyclosporin A and mass spectrometric sequencing of tryptic peptides confirmed its classification as a cyclophilin. Genes encoding similar putative thylakoid cyclophilins with a unique insert of three amino acids NPV in their N-termini were found in chromosome 5 of both Arabidopsis and rice. TLP20 is suggested to be the major PPIase and protein folding catalyst in the thylakoid lumen of plant chloroplasts.

  • 3. Erling Tjus, Staffan
    et al.
    Vibe Scheller, Henrik
    Andersson, Bertil
    Linköping University, Faculty of Health Sciences. Linköping University, Department of Biomedicine and Surgery, Cell biology.
    Lindberg Möller, Birger
    Active oxygen produced during selective excitation of photosystem I is damaging not only to photosystem I, but also to photosystem II.2001In: Plant Physiology, ISSN 0032-0889, E-ISSN 1532-2548, Vol. 125, p. 2007-2015Article in journal (Refereed)
  • 4.
    Hansson, Maria
    et al.
    Linköping University, Department of Clinical and Experimental Medicine, Cell Biology. Linköping University, Faculty of Health Sciences.
    Dupuis, Tiphaine
    Department of Biochemistry and Biophysics, Arrhenius Laboratories for Natural Sciences, Stockholm University, Stockholm, Sweden .
    Strömquist, Ragna
    Department of Biochemistry and Biophysics, Arrhenius Laboratories for Natural Sciences, Stockholm University, Stockholm, Sweden .
    Andersson, Bertil
    Linköping University, Department of Clinical and Experimental Medicine, Cell Biology. Linköping University, Faculty of Health Sciences.
    Vener, Alexander V.
    Linköping University, Department of Clinical and Experimental Medicine, Cell Biology. Linköping University, Faculty of Health Sciences.
    Carlberg, Inger
    Department of Biochemistry and Biophysics, Arrhenius Laboratories for Natural Sciences, Stockholm University, Stockholm, Sweden .
    The mobile thylakoid phosphoprotein TSP9 interacts with the light harvesting complex II and the peripheries of both photosystems2006In: Journal of Biological Chemistry, ISSN 0021-9258, Vol. 282, no 22, p. 16214-16222Article in journal (Refereed)
    Abstract [en]

    The localization of the plant-specific thylakoid-soluble phosphoprotein of 9 kDa, TSP9, within the chloroplast thylakoid membrane of spinach has been established by the combined use of fractionation, immunoblotting, cross-linking, and mass spectrometry. TSP9 was found to be exclusively confined to the thylakoid membranes, where it is enriched in the stacked grana membrane domains. After mild solubilization of the membranes, TSP9 migrated together with the major light-harvesting antenna (LHCII) of photosystem II (PSII) and with PSII-LHCII supercomplexes upon separation of the protein complexes by either native gel electrophoresis or sucrose gradient centrifugation. Studies with a cleavable cross-linking agent revealed the interaction of TSP9 with both major and minor LHCII proteins as identified by mass spectrometric sequencing. Cross-linked complexes that in addition to TSP9 contain the peripheral PSII subunits CP29, CP26, and PsbS, which form the interface between LHCII and the PSII core, were found. Our observations also clearly suggest an interaction of TSP9 with photosystem I (PSI) as shown by both immunodetection and mass spectrometry. Sequencing identified the peripheral PSI subunits PsaL, PsaF, and PsaE, originating from cross-linked protein complexes of around 30 kDa that also contained TSP9. The distribution of TSP9 among the cross-linked forms was found to be sensitive to conditions such as light exposure. An association of TSP9 with LHCII as well as the peripheries of the photosystems suggests its involvement in regulation of photosynthetic light harvesting.

  • 5. Haussühl, Kirsten
    et al.
    Andersson, Bertil
    Linköping University, Faculty of Health Sciences. Linköping University, Department of Biomedicine and Surgery, Cell biology.
    Adamska, Iwona
    A chloroplast DegP2 protease performs the primary cleavage of the photodamaged D1 protein in plant photosystem II2001In: EMBO Journal, ISSN 0261-4189, E-ISSN 1460-2075, Vol. 20, no 4, p. 713-722Article in journal (Refereed)
    Abstract [en]

    Although light is the ultimate substrate in photosynthesis, it can also be harmful and lead to oxidative damage of the photosynthetic apparatus. The main target for light stress is the central oxygen-evolving photosystem II (PSII) and its D1 reaction centre protein. Degradation of the damaged D1 protein and its rapid replacement by a de novo synthesized copy represent the important repair mechanism of PSII crucial for plant survival under light stress conditions. Here we report the isolation of a single-copy nuclear gene from Arabidopsis thaliana, encoding a protease that performs GTP-dependent primary cleavage of the photodamaged D1 protein and hence catalysing the key step in the repair cycle in plants. This protease, designated DegP2, is a homologue of the prokaryotic Deg/Htr family of serine endopeptidases and is associated with the stromal side of the non-appressed region of the thylakoid membranes. Increased expression of DegP2 under high salt, desiccation and light stress conditions was measured at the protein level.

  • 6.
    Heddad, Mounia
    et al.
    Stockholm University.
    Noren, Hanna
    Stockholm University.
    Reiser, Verena
    University of Konstanz.
    Dunaeva, Marina
    Stockholm University.
    Andersson, Bertil
    Linköping University, Department of Clinical and Experimental Medicine, Cell Biology. Linköping University, Faculty of Health Sciences.
    Adamska, Iwona
    University of Konstanz, Germany.
    Differential expression and localization of early light-induced proteins in Arabidopsis2006In: Plant Physiology, ISSN 0032-0889, E-ISSN 1532-2548, Vol. 142, no 1, p. 75-87Article in journal (Refereed)
    Abstract [en]

    The early light-induced proteins (Elips) in higher plants are nuclear-encoded, light stress-induced proteins located in thylakoid membranes and related to light-harvesting chlorophyll (LHC) a/b-binding proteins. A photoprotective function was proposed for Elips. Here we showed that after 2 h exposure of Arabidopsis (Arabidopsis thaliana) leaves to light stress Elip1 and Elip2 coisolate equally with monomeric (mLhcb) and trimeric (tLhcb) populations of the major LHC from photosystem II (PSII) as based on the Elip:Lhcb protein ratio. A longer exposure to light stress resulted in increased amounts of Elips in tLhcb as compared to mLhcb, due to a reduction of tLhcb amounts. We demonstrated further that the expression of Elip1 and Elip2 transcripts was differentially regulated in green leaves exposed to light stress The accumulation of Elip1 transcripts and proteins increased almost linearly with increasing light intensities and correlated with the degree of photoinactivation and photodamage of PSII reaction centers. A stepwise accumulation of Elip2 was induced when 40% of PSII reaction centers became photodamaged. The differential expression of Elip1 and Elip2 occurred also in light stress-preadapted or senescent leaves exposed to light stress but there was a lack of correlation between transcript and protein accumulation. Also in this system the accumulation of Elip1 but not Elip2 correlated with the degree of PSII photodamage. Based on pigment analysis, measurements of PSII activity, and assays of the oxidation status of proteins we propose that the discrepancy between amounts of Elip transcripts and proteins in light stress-preadapted or senescent leaves is related to a presence of photoprotective anthocyanins or to lower chlorophyll availability, respectively

  • 7.
    Huang, F
    et al.
    Stockholm University.
    Parmryd, I
    Stockholm University.
    Nilsson, F
    AstraZeneca R&D .
    Persson, AL
    Stockholm University.
    Pakrasi, HB
    Washington University.
    Andersson, Bertil
    Linköping University, Department of Physics, Chemistry and Biology. Linköping University, The Institute of Technology.
    Norling, B
    Stockholm University.
    Proteomics of Synechocystis sp strain PCC 6803 - Identification of plasma membrane proteins2002In: Molecular & Cellular Proteomics, ISSN 1535-9476, E-ISSN 1535-9484, Vol. 1, no 12, p. 956-966Article in journal (Refereed)
    Abstract [en]

    Cyanobacteria are unique prokaryotes since they in addition to outer and plasma membranes contain the photosynthetic membranes (thylakoids) The plasma membranes of Synechocystis 6803, which can be completely purified by density centrifugation and polymer two-phase partitioning, have been found to be more complex than previously anticipated, i. e they appear to be essential for assembly of the two photosystems. A proteomic approach for the characterization of cyanobacterial plasma membranes using two-dimensional gel electrophoresis and mass spectrometry analysis revealed a total of 57 different membrane proteins of which 17 are integral membrane spanning proteins. Among the 40 peripheral proteins 20 are located on the periplasmic side of the membrane, while 20 are on the cytoplasmic side. Among the proteins identified are subunits of the two photosystems as well as Vipp1, which has been suggested to be involved in vesicular transport between plasma and thylakoid membranes and is thus relevant to the possibility that plasma membranes are the initial site for photosystem biogenesis. Four subunits of the Pilus complex responsible for cell motility were also identified as well as several subunits of the TolC and TonB transport systems. Several periplasmic and ATP-binding proteins of ATP-binding cassette transporters were also identified as were two subunits of the F-0 membrane part of the ATP synthase

  • 8. 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.

  • 9. 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.

  • 10. Mamedov, Fikret
    et al.
    Rintamäki, Eevi
    Aro, Eva-Mari
    Andersson, Bertil
    Linköping University, Faculty of Health Sciences. Linköping University, Department of Biomedicine and Surgery, Cell biology.
    Styring, Stenbjörn
    Influence of protein phosphorylation on the electron-transport properties of Photosystem II2002In: Photosynthesis Research, ISSN 0166-8595, E-ISSN 1573-5079, Vol. 74, no 1, p. 61-72Article in journal (Refereed)
    Abstract [en]

    Many of the core proteins in Photosystem II (PS II) undergo reversible phosphorylation. It is known that protein phosphorylation controls the repair cycle of Photosystem II. However, it is not known how protein phosphorylation affects the partial electron transport reactions in PS II. Here we have applied variable fluorescence measurements and EPR spectroscopy to probe the status of the quinone acceptors, the Mn cluster and other electron transfer components in PS II with controlled levels of protein phosphorylation. Protein phosphorylation was induced in vivo by varying illumination regimes. The phosphorylation level of the D1 protein varied from 10 to 58% in PS II membranes isolated from pre-illuminated spinach leaves. The oxygen evolution and QA- to QB(QB-) electron transfer measured by flash-induced fluorescence decay remained similar in all samples studied. Similar measurements in the presence of DCMU, which reports on the status of the donor side in PS II, also indicated that the integrity of the oxygen-evolving complex was preserved in PS II with different levels of D1 protein phosphorylation. With EPR spectroscopy we examined individual redox cofactors in PS II. Both the maximal amplitude of the charge separation reaction (measured as photo-accumulated pheophytin-) and the EPR signal from the QA- Fe2+ complex were unaffected by the phosphorylation of the D1 protein, indicating that the acceptor side of PS II was not modified. Also the shape of the S2 state multiline signal was similar, suggesting that the structure of the Mn-cluster in Photosystem II did not change. However, the amplitude of the S2 multiline signal was reduced by 35% in PS II, where 58% of the D1 protein was phosphorylated, as compared to the S2 multiline in PS II, where only 10% of the D1 protein was phosphorylated. In addition, the fraction of low potential Cyt b559 was twice as high in phosphorylated PS II. Implications from these findings, were precise quantification of D1 protein phosphorylation is, for the first time, combined with high-resolution biophysical measurements, are discussed.

  • 11.
    Noren, H
    et al.
    Stockholm University.
    Svensson, P
    The Swedish University of Agricultural Sciences.
    Andersson, Bertil
    Linköping University, Department of Physics, Chemistry and Biology. Linköping University, The Institute of Technology.
    A convenient and versatile hydroponic cultivation system for Arabidopsis thaliana2004In: Physiologia Plantarum: An International Journal for Plant Biology, ISSN 0031-9317, E-ISSN 1399-3054, Vol. 121, no 3, p. 343-348Article in journal (Refereed)
    Abstract [en]

    A versatile two-step cultivation procedure for Arabidopsis thaliana is described for the production of large quantities of leaf material suitable for biochemical and biophysical analysis. The first step comprises a miniature greenhouse made out of a plastic pipette box to grow the seedlings to the six-leaf stage. For continued growth, the seedlings are transferred to hydroponic cultivation using an opaque container covered by a styrofoam lid. Transfer of the small seedlings to hydroponic culture is facilitated by growth in separate pipette tips, which protects vulnerable roots from damage. The hydroponic cultivation system is easy to scale-up and produces large amounts of relatively large leaves and roots. This hydroponic system produces enough plant material to make Arabidopsis a feasible model for biochemical and biophysical experiments, which can be combined with the available genetic information to address various aspects of plant functional genomics

  • 12.
    Noren, H.
    et al.
    Norén, H., Dept. of Biochemistry and Biophysics, Arrhenius Labs. for Natural Sciences, Stockholm University, SE-10691 Stockholm, Sweden.
    Svensson, P.
    Department of Plant Biology, Swedish Agricultural University, Box 7080, SE-75007 Uppsala, Sweden.
    Stegmark, R.
    Findus R and D AB, SE-26725 Bjuv, Sweden.
    Funk, C.
    Dept. of Biochemistry and Biophysics, Arrhenius Labs. for Natural Sciences, Stockholm University, SE-10691 Stockholm, Sweden, Department of Biochemistry, Umeå University, SE-90187 Umeå, Sweden.
    Adamska, I.
    Dept. of Biochemistry and Biophysics, Arrhenius Labs. for Natural Sciences, Stockholm University, SE-10691 Stockholm, Sweden.
    Andersson, B.
    Linköping University, Department of Physics, Chemistry and Biology. Linköping University, The Institute of Technology.
    Expression of the early light-induced protein but not the PsbS protein is influenced by low temperature and depends on the developmental stage of the plant in field-grown pea cultivars2003In: Plant, Cell and Environment, ISSN 0140-7791, E-ISSN 1365-3040, Vol. 26, no 2, p. 245-253Article in journal (Refereed)
    Abstract [en]

    Plant cells exposed to photo-inhibitory conditions respond by accumulation of the early light-induced proteins (Elips) with a potential photoprotective function. Here we studied the expression of Elip in various pea cultivars grown under agricultural or climate-chamber conditions. We demonstrated that the expression of Elip in all cultivars was developmentally regulated and its level decreased during flowering and post-flowering periods. Surprisingly, significant amounts of Elip transcripts, but not proteins, accumulated in senescing leaves already under low light conditions and the exposure to light stress resulted in a 10-times higher induction of Elip transcripts. Furthermore, the expression pattern of Elip transcript and protein significantly differed under field and growth-chamber conditions. First, the expression level of Elip was much higher in field-grown than in chamber-grown cultivars. Second, substantial amounts of Elip transcripts and protein were detected during the night in field-grown plants in contrast to chamber-grown cultivars due to a synergistic effect of light stress occurring during the day and low temperature present during the following night. The expression of the PsbS protein related to Elips and involved in the photoprotection of the photosystem II was relatively constant under all conditions tested.

  • 13. Rokka, Anne
    et al.
    Aro, Eva-Mari
    Herrmann, Reinhold
    Andersson, Bertil
    Linköping University, Faculty of Health Sciences. Linköping University, Department of Biomedicine and Surgery, Cell biology.
    Vener, Alexander
    Linköping University, Faculty of Health Sciences. Linköping University, Department of Biomedicine and Surgery, Cell biology.
    Dephosphorylation of photosystem II reaction center proteins in plant photosynthetic membranes as an immediate response to abrupt elevation of temperature.2000In: Plant Physiology, ISSN 0032-0889, E-ISSN 1532-2548, Vol. 123, p. 1525-1535Article in journal (Refereed)
  • 14.
    Romano, Patrick G.N.
    et al.
    Department of Molecular Biology and Biotechnology, University of Sheffield, Western Bank, Sheffield, United Kingdom.
    Edvardsson, Anna
    Linköping University, Department of Clinical and Experimental Medicine, Cell Biology. Linköping University, Faculty of Health Sciences.
    Ruban, Alexander V.
    Andersson, Bertil
    Department of Biochemistry and Biophysics, Arrhenius Laboratories for Natural Sciences, Stockholm University, Stockholm, Sweden .
    Vener, Alexander
    Linköping University, Department of Clinical and Experimental Medicine, Cell Biology. Linköping University, Faculty of Health Sciences.
    Gray, Julie E.
    Department of Molecular Biology and Biotechnology, University of Sheffield, Western Bank, Sheffield, United Kingdom.
    Horton, Peter
    Department of Molecular Biology and Biotechnology, University of Sheffield, Western Bank, Sheffield, United Kingdom.
    Arabidopsis AtCYP20-2 is a light-regulated cyclophilin-type peptidyl-prolyl cis-trans isomerase associated with the photosynthetic membranes2004In: Plant Physiology, ISSN 0032-0889, Vol. 134, no 4, p. 1244-1247Article in journal (Refereed)
  • 15.
    Shutova, T
    et al.
    Umeå University.
    Klimov, VV
    Russian Academy of Sciences.
    Andersson, Bertil
    Linköping University, Department of Clinical and Experimental Medicine, Cell Biology. Linköping University, Faculty of Health Sciences.
    Samuelsson, G
    Umeå University.
    A cluster of carboxylic groups in PsbO protein is involved in proton transfer from the water oxidizing complex of Photosystem II2007In: Biochimica et Biophysica Acta - Bioenergetics, ISSN 0005-2728, E-ISSN 1879-2650, Vol. 1767, no 6, p. 434-440Article in journal (Refereed)
    Abstract [en]

    The hypothesis presented here for proton transfer away from the water oxidation complex of Photosystem II (PSII) is supported by biochemical experiments on the isolated PsbO protein in solution, theoretical analyses of better understood proton transfer systems like bacteriorhodopsin and cytochrome oxidase, and the recently published 3D structure of PS II (Pdb entry IS5L). We propose that a cluster of conserved glutamic and aspartic acid residues in the PsbO protein acts as a buffering network providing efficient acceptors of protons derived from substrate water molecules. The charge delocalization of the cluster ensures readiness to promptly accept the protons liberated from substrate water. Therefore protons generated at the catalytic centre of PSII need not be released into the thylakoid lumen as generally thought. The cluster is the beginning of a localized, fast proton transfer conduit on the lumenal side of the thylakoid membrane Proton-dependent conformational changes of PsbO may play a role in the regulation of both supply of substrate water to the water oxidizing complex and the resultant proton transfer.

  • 16.
    Shutova, T
    et al.
    Umeå University.
    Nikitina, J
    Umeå University.
    Deikus, G
    New York University.
    Andersson, Bertil
    Linköping University, Department of Clinical and Experimental Medicine, Cell Biology. Linköping University, Faculty of Health Sciences.
    Klimov, V
    Russian Academy of Sciences.
    Samuelsson, G
    Umeå University.
    Structural dynamics of the manganese-stabilizing protein - Effect of pH, calcium, and manganese2005In: Biochemistry, ISSN 0006-2960, E-ISSN 1520-4995, Vol. 44, no 46, p. 15182-15192Article in journal (Refereed)
    Abstract [en]

    The photosystem-II-associated 33-kDa extrinsic manganese-stabilizing protein is found in all oxygen-evolving organisms. In this paper, we show that this protein undergoes pH-induced conformational changes in the physiological pH range. At a neutral pH of 7.2, the hydrophobic amino acid residues that are most likely located inside the beta barrel are "closed" and the protein binds neither Mn2+ nor Ca2+ ions. When the protein is transferred to a solution with a slightly acidic pH of 5.7, hydrophobic amino acid residues become exposed to the surrounding medium, enabling them to bind the fluorescent probe 8,1-ANS. At this pH-induced open state, Mn2+ and Ca2+ bind to the manganese-stabilizing protein. The pH values used in this study, 7.2 and 5.7, are typical of the pH found in the thylakoid lumen in the dark and light, respectively. A model is presented in which the manganese-stabilizing protein undergoes a pH-dependent conformational change that in turn influences its capacity to bind calcium and manganese. In this model, the proton-dependent conformational changes of the tertiary structure of the manganese-stabilizing protein are of functional relevance for the regulation of substrate (water) delivery to and product (proton) release from the water-oxidizing complex by forming a proton-sensing proton-transport pathway

  • 17.
    Shutova, Tatiana
    et al.
    Umea Univ, Dept Plant Physiol, Umea Plant Sci Ctr, S-90187 Umea, Sweden.
    Kenneweg, Hella
    Univ Osnabruck, Dept Biophys, Osnabruck, Germany.
    Buchta, Joachim
    Free Univ Berlin, Dept Phys, D-1000 Berlin, Germany.
    Nikitina, Julia
    Russian Acad Sci, Inst Basic Biol Problems, Pushchino 142292, Russia.
    Terentyev, Vasily
    Russian Acad Sci, Inst Basic Biol Problems, Pushchino 142292, Russia.
    Chernyshov, Sergey
    Russian Acad Sci, Branch Shemyakin & Ovchinnikov, Inst Bioorgan Chem, Pushchino 142292, Russia.
    Andersson, Bertil
    Linköping University, Department of Clinical and Experimental Medicine, Cell Biology. Linköping University, Faculty of Health Sciences.
    Allakhverdiev, Suleyman I.
    Russian Acad Sci, Inst Basic Biol Problems, Pushchino 142292, Russia.
    Klimov, Vyacheslav V.
    Russian Acad Sci, Inst Basic Biol Problems, Pushchino 142292, Russia.
    Dau, Holger
    Free Univ Berlin, Dept Phys, D-1000 Berlin, Germany.
    Junge, Wolfgang
    Univ Osnabruck, Dept Biophys, Osnabruck, Germany.
    Samuelsson, Goran
    Umea Univ, Dept Plant Physiol, Umea Plant Sci Ctr, S-90187 Umea, Sweden.
    The photosystem II-associated Cah3 in Chlamydomonas enhances the O-2 evolution rate by proton removal2008In: EMBO Journal, ISSN 0261-4189, E-ISSN 1460-2075, Vol. 27, no 5, p. 782-791Article in journal (Refereed)
    Abstract [en]

    Water oxidation in photosystem II ( PSII) is still insufficiently understood and is assumed to involve HCO3-. A Chlamydomonas mutant lacking a carbonic anhydrase associated with the PSII donor side shows impaired O-2 evolution in the absence of HCO3-. The O-2 evolution for saturating, continuous illumination (R-O2) was slower than in the wild type, but was elevated by HCO3- and increased further by Cah3. The R-O2 limitation in the absence of Cah3/HCO3- was amplified by H2O/D2O exchange, but relieved by an amphiphilic proton carrier, suggesting a role of Cah3/HCO3- in proton translocation. Chlorophyll fluorescence indicates a Cah3/HCO3- effect at the donor side of PSII. Time-resolved delayed fluorescence and O-2-release measurements suggest specific effects on proton-release steps but not on electron transfer. We propose that Cah3 promotes proton removal from the Mn complex by locally providing HCO3-, which may function as proton carrier. Without Cah3, proton removal could become rate limiting during O-2 formation and thus, limit water oxidation under high light. Our results underlie the general importance of proton release at the donor side of PSII during water oxidation.

  • 18.
    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.

  • 19.
    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.

  • 20. Yang, Dan-Hui
    et al.
    Andersson, Bertil
    Linköping University, Faculty of Health Sciences. Linköping University, Department of Biomedicine and Surgery, Cell biology.
    Aro, Eva-Mari
    Ohad, Itzhak
    The redox state of the plastoquinone pool controls the level of the light-harvesting chlorophyll a/b binding protein complex II (LHC II) during photoacclimation.2001In: Photosynthesis Research, ISSN 0166-8595, E-ISSN 1573-5079, Vol. 68, p. 163-174Article in journal (Refereed)
  • 21. Yang, Dan-Hui
    et al.
    Paulsen, Harald
    Andersson, Bertil
    Linköping University, Faculty of Health Sciences. Linköping University, Department of Biomedicine and Surgery, Cell biology.
    The N-terminal domain of the light-harvesting chlorophyll a/b-binding protein complex (LHCII) is essential for its acclimative proteolysis2000In: FEBS Letters, ISSN 0014-5793, E-ISSN 1873-3468, Vol. 466, no 2-3, p. 385-388Article in journal (Refereed)
    Abstract [en]

    Variations in the amount of the light-harvesting chlorophyll a/b-binding protein complex (LHCII) is essential for regulation of the uptake of light into photosystem II. An endogenous proteolytic system was found to be involved in the degradation of LHCII in response to elevated light intensities and the proteolysis was shown to be under tight regulation [Yang, D.-H. et al. (1998) Plant Physiol. 118, 827-834]. In this study, the substrate specificity and recognition site towards the protease were examined using reconstituted wild-type and mutant recombinant LHCII. The results show that the LHCII apoprotein and the monomeric form of the holoprotein are targeted for proteolysis while the trimeric form is not. The N-terminal domain of LHCII was found to be essential for recognition by the regulatory protease and the involvement of the N-end rule pathway is discussed. (C) 2000 Federation of European Biochemical Societies.

  • 22.
    Yang, DH
    et al.
    Stockholm University.
    Andersson, Bertil
    Linköping University, Department of Physics, Chemistry and Biology. Linköping University, The Institute of Technology.
    Aro, EM
    University of Turku.
    Ohad, I
    The Hebrew University of Jerusalem.
    The redox state of the plastoquinone pool controls the level of the light-harvesting chlorophyll a/b binding protein complex II (LHC II) during photoacclimation - Cytochrome b(6)f deficient Lemna perpusilla plants are locked in a state of high-light acclimation2001In: Photosynthesis Research, ISSN 0166-8595, E-ISSN 1573-5079, Vol. 68, no 2, p. 163-174Article in journal (Refereed)
    Abstract [en]

    A cytochrome bf deficient mutant of Lemna perpusilla maintains a constant and lower level of the light-harvesting chl a/b-binding protein complex II (LHC II) as compared to the wild type plants at low-light intensities. Inhibition of the plastoquinone pool reduction increases the LHC II content of the mutant at both low- and high-light intensities but only at high-light intensity in the wild type plants Proteolytic activity against LHC II appears during high-light photoacclimation of wild type plants. However, the acclimative protease is present in the mutant at both light intensities. These and additional results suggest that the plastoquinone redox state serves as the major signal-transducing component in the photoacclimation process affecting both, synthesis and degradation of LHC II and appearance of acclimative LHC II proteolysis. The plastoquinol pool cannot be oxidized by linear electron flow in the mutant plants which are locked in a `high light acclimation state. The cytochrome bf complex may be involved indirectly in the regulation of photoacclimation via 1) regulation of the plastoquinone redox state; 2) regulation of the redox-controlled thylakoid protein kinase allowing exposure of the dephosphorylated LHC II to acclimative proteolysis

  • 23. Zak, Elena
    et al.
    Norling, Birgitta
    Maitra, Radhashree
    Huang, Fang
    Andersson, Bertil
    Linköping University, Faculty of Health Sciences. Linköping University, Department of Biomedicine and Surgery, Cell biology.
    Pakrasi, Himadri
    The initial steps of biogenesis of cyanobacterial photosystems occur in plasma membranes2001In: Proceedings of the National Academy of Sciences of the United States of America, ISSN 0027-8424, E-ISSN 1091-6490, Vol. 98, no 23, p. 13443-13448Article in journal (Refereed)
    Abstract [en]

    During oxygenic photosynthesis in cyanobacteria and chloroplasts of plants and eukaryotic algae, conversion of light energy to biologically useful chemical energy occurs in the specialized thylakoid membranes. Light-induced charge separation at the reaction centers of photosystems I and II, two multisubunit pigment-protein complexes in the thylakoid membranes, energetically drive sequential photosynthetic electron transfer reactions in this membrane system. In general, in the prokaryotic cyanobacterial cells, the thylakoid membrane is distinctly different from the plasma membrane. We have recently developed a two-dimensional separation procedure to purify thylakoid and plasma membranes from the genetically widely studied cyanobacterium Synechocystis sp. PCC 6803. Immunoblotting analysis demonstrated that the purified plasma membrane contained a number of protein components closely associated with the reaction centers of both photosystems. Moreover, these proteins were assembled in the plasma membrane as chlorophyll-containing multiprotein complexes, as evidenced from nondenaturing green gel and low-temperature fluorescence spectroscopy data. Furthermore, electron paramagnetic resonance spectroscopic analysis showed that in the partially assembled photosystem I core complex in the plasma membrane, the P700 reaction center was capable of undergoing light-induced charge separation. Based on these data, we propose that the plasma membrane, and not the thylakoid membrane, is the site for a number of the early steps of biogenesis of the photosynthetic reaction center complexes in these cyanobacterial cells.

  • 24.
    Zer, H.
    et al.
    Department of Biological Chemistry, Hebrew University of Jerusalem, Jerusalem 91904, Israel.
    Vink, M.
    Department of Biochemistry, Arrhenius Laboratories, Stockholm University, SE-106 91 Stockholm, Sweden.
    Shochat, S.
    Department of Biological Chemistry, Hebrew University of Jerusalem, Jerusalem 91904, Israel.
    Herrmann, R.G.
    Institute of Botany, Ludwig Maximilians University, D-80638 Münich, Germany.
    Andersson, B.
    Linköping University, Department of Physics, Chemistry and Biology. Linköping University, The Institute of Technology.
    Ohad, I.
    Department of Biological Chemistry, Hebrew University of Jerusalem, Jerusalem 91904, Israel.
    Light affects the accessibility of the thylakoid light harvesting complex II (LHCII) phosphorylation site to the membrane protein kinase(s)2003In: Biochemistry, ISSN 0006-2960, E-ISSN 1520-4995, Vol. 42, no 3, p. 728-738Article in journal (Refereed)
    Abstract [en]

    Redox-controlled, reversible phosphorylation of the thylakoid light harvesting complex II (LHCII) regulates its association with photosystems (PS) I or II and thus, energy distribution between the two photosystems (state transition). Illumination of solubilized LHCII enhances exposure of the phosphorylation site at its N-terminal domain to protein kinase(s) and tryptic cleavage in vitro [Zer et al. (1999) Proc. Natl. Acad. Sci. U.S.A. 96, 8277-8282]. Here we report that short illumination (5-10 min, 15-30, µmol m-2 s-1) enhances the accessibility of LHCII phosphorylation site to kinase(s) activity also in isolated thylakoids. However, prolonged illumination or higher light intensities (30 min, 80-800 µmol m-2 s-1) prevent phosphorylation of LHCII in the isolated membranes as well as in vivo, although redox-dependent protein kinase activity persists in the illuminated thylakoids toward exogenous solubilized LHCII. This phenomenon, ascribed to light-induced inaccessibility of the phosphorylation site to the protein kinase(s), affects in a similar way the accessibility of thylakoid LHCII N-terminal domain to tryptic cleavage. The illumination effect is not redox related, decreases linearly with temperature from 25 to 5°C and may be ascribed to light-induced conformational changes in the complex causing lateral aggregation of dephosphorylated LHCII bound to and/or dissociated from PSII. The later state occurs under conditions allowing turnover of the phospho-LHCII phosphate. The light-induced inaccessibility of LHCII to the membrane-bound protein kinase reverses readily in darkness only if induced under LHCII-phosphate turnover conditions. Thus, phosphorylation prevents irreversible light-induced conformational changes in LHCII allowing lateral migration of the complex and the related state transition process.

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