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BETA
Andersson, Bertil
Alternative names
Publications (10 of 24) Show all publications
Shutova, T., Kenneweg, H., Buchta, J., Nikitina, J., Terentyev, V., Chernyshov, S., . . . Samuelsson, G. (2008). The photosystem II-associated Cah3 in Chlamydomonas enhances the O-2 evolution rate by proton removal. EMBO Journal, 27(5), 782-791
Open this publication in new window or tab >>The photosystem II-associated Cah3 in Chlamydomonas enhances the O-2 evolution rate by proton removal
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2008 (English)In: EMBO Journal, ISSN 0261-4189, E-ISSN 1460-2075, Vol. 27, no 5, p. 782-791Article in journal (Refereed) Published
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.

Keywords
carbonic anhydrase, Chlamydomonas reinhardtii, photosystem II, proton removal, water oxidation
National Category
Natural Sciences
Identifiers
urn:nbn:se:liu:diva-45905 (URN)10.1038/emboj.2008.12 (DOI)
Available from: 2009-10-11 Created: 2009-10-11 Last updated: 2017-12-13
Shutova, T., Klimov, V., Andersson, B. & Samuelsson, G. (2007). A cluster of carboxylic groups in PsbO protein is involved in proton transfer from the water oxidizing complex of Photosystem II. Biochimica et Biophysica Acta - Bioenergetics, 1767(6), 434-440
Open this publication in new window or tab >>A cluster of carboxylic groups in PsbO protein is involved in proton transfer from the water oxidizing complex of Photosystem II
2007 (English)In: Biochimica et Biophysica Acta - Bioenergetics, ISSN 0005-2728, E-ISSN 1879-2650, Vol. 1767, no 6, p. 434-440Article in journal (Refereed) Published
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.

Keywords
Photosystem II; PsbO protein; proton transfer; cluster of carboxylic group
National Category
Engineering and Technology
Identifiers
urn:nbn:se:liu:diva-53631 (URN)10.1016/j.bbabio.2007.01.020 (DOI)
Available from: 2010-01-26 Created: 2010-01-26 Last updated: 2017-12-12
Heddad, M., Noren, H., Reiser, V., Dunaeva, M., Andersson, B. & Adamska, I. (2006). Differential expression and localization of early light-induced proteins in Arabidopsis. Plant Physiology, 142(1), 75-87
Open this publication in new window or tab >>Differential expression and localization of early light-induced proteins in Arabidopsis
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2006 (English)In: Plant Physiology, ISSN 0032-0889, E-ISSN 1532-2548, Vol. 142, no 1, p. 75-87Article in journal (Refereed) Published
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

National Category
Engineering and Technology
Identifiers
urn:nbn:se:liu:diva-53634 (URN)10.1104/pp.106.081489 (DOI)
Available from: 2010-01-26 Created: 2010-01-26 Last updated: 2017-12-12
Hansson, M., Dupuis, T., Strömquist, R., Andersson, B., Vener, A. V. & Carlberg, I. (2006). The mobile thylakoid phosphoprotein TSP9 interacts with the light harvesting complex II and the peripheries of both photosystems. Journal of Biological Chemistry, 282(22), 16214-16222
Open this publication in new window or tab >>The mobile thylakoid phosphoprotein TSP9 interacts with the light harvesting complex II and the peripheries of both photosystems
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2006 (English)In: Journal of Biological Chemistry, ISSN 0021-9258, Vol. 282, no 22, p. 16214-16222Article in journal (Refereed) Published
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.

National Category
Medical and Health Sciences
Identifiers
urn:nbn:se:liu:diva-13862 (URN)10.1074/jbc.M605833200 (DOI)
Available from: 2006-09-07 Created: 2006-09-07 Last updated: 2010-05-24
Shutova, T., Nikitina, J., Deikus, G., Andersson, B., Klimov, V. & Samuelsson, G. (2005). Structural dynamics of the manganese-stabilizing protein - Effect of pH, calcium, and manganese. Biochemistry, 44(46), 15182-15192
Open this publication in new window or tab >>Structural dynamics of the manganese-stabilizing protein - Effect of pH, calcium, and manganese
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2005 (English)In: Biochemistry, ISSN 0006-2960, E-ISSN 1520-4995, Vol. 44, no 46, p. 15182-15192Article in journal (Refereed) Published
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

National Category
Engineering and Technology
Identifiers
urn:nbn:se:liu:diva-53637 (URN)10.1021/bi0512750 (DOI)
Available from: 2010-01-26 Created: 2010-01-26 Last updated: 2017-12-12
Noren, H., Svensson, P. & Andersson, B. (2004). A convenient and versatile hydroponic cultivation system for Arabidopsis thaliana. Physiologia Plantarum: An International Journal for Plant Biology, 121(3), 343-348
Open this publication in new window or tab >>A convenient and versatile hydroponic cultivation system for Arabidopsis thaliana
2004 (English)In: 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) Published
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

National Category
Engineering and Technology
Identifiers
urn:nbn:se:liu:diva-53639 (URN)10.1111/j.0031-9317.2004.00350.x (DOI)
Available from: 2010-01-26 Created: 2010-01-26 Last updated: 2017-12-12
Romano, P. G. .., Edvardsson, A., Ruban, A. V., Andersson, B., Vener, A., Gray, J. E. & Horton, P. (2004). Arabidopsis AtCYP20-2 is a light-regulated cyclophilin-type peptidyl-prolyl cis-trans isomerase associated with the photosynthetic membranes. Plant Physiology, 134(4), 1244-1247
Open this publication in new window or tab >>Arabidopsis AtCYP20-2 is a light-regulated cyclophilin-type peptidyl-prolyl cis-trans isomerase associated with the photosynthetic membranes
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2004 (English)In: Plant Physiology, ISSN 0032-0889, Vol. 134, no 4, p. 1244-1247Article in journal (Refereed) Published
National Category
Medical and Health Sciences
Identifiers
urn:nbn:se:liu:diva-14356 (URN)10.1104/pp.104.041186 (DOI)
Available from: 2007-04-10 Created: 2007-04-10 Last updated: 2009-05-29
Spetea Wiklund, C., Hundal, T., Lundin, B., Heddad, M., Adamska, I. & Andersson, B. (2004). Multiple evidence for nucleotide metabolism in the chloroplast thylakoid lumen. Proceedings of the National Academy of Science, 101(5), 1409-1414
Open this publication in new window or tab >>Multiple evidence for nucleotide metabolism in the chloroplast thylakoid lumen
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2004 (English)In: Proceedings of the National Academy of Science, ISSN 0027-8424, Vol. 101, no 5, p. 1409-1414Article in journal (Refereed) Published
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.

National Category
Natural Sciences
Identifiers
urn:nbn:se:liu:diva-13003 (URN)10.1073/pnas.0308164100 (DOI)
Available from: 2008-03-20 Created: 2008-03-20 Last updated: 2010-01-26
Carlberg, I., Hansson, M., Kieselbach, T., Schröder, W. P., Andersson, B. & Vener, A. V. (2003). A novel plant protein undergoing light-induced phosphorylation and release from the photosynthetic thylakoid membranes. Proceedings of the National Academy of Sciences of the United States of America, 100(2), 757-762
Open this publication in new window or tab >>A novel plant protein undergoing light-induced phosphorylation and release from the photosynthetic thylakoid membranes
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2003 (English)In: 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) Published
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.

Place, publisher, year, edition, pages
National Academy of Sciences, 2003
National Category
Medical and Health Sciences
Identifiers
urn:nbn:se:liu:diva-13861 (URN)10.1073/pnas.0235452100 (DOI)
Available from: 2006-09-07 Created: 2006-09-07 Last updated: 2017-12-13Bibliographically approved
Kanervo, E., Spetea, C., Nishiyama, Y., Murata, N., Andersson, B. & Aro, E.-M. (2003). Dissecting a cyanobacterial proteolytic system: Efficiency in inducing degradation of the D1 protein of photosystem II in cyanobacteria and plants. Biochimica et Biophysica Acta - Bioenergetics, 1607(2-3), 131-140
Open this publication in new window or tab >>Dissecting a cyanobacterial proteolytic system: Efficiency in inducing degradation of the D1 protein of photosystem II in cyanobacteria and plants
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2003 (English)In: Biochimica et Biophysica Acta - Bioenergetics, ISSN 0005-2728, E-ISSN 1879-2650, Vol. 1607, no 2-3, p. 131-140Article in journal (Refereed) Published
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.

National Category
Medical and Health Sciences
Identifiers
urn:nbn:se:liu:diva-24857 (URN)10.1016/j.bbabio.2003.09.007 (DOI)9258 (Local ID)9258 (Archive number)9258 (OAI)
Available from: 2009-10-07 Created: 2009-10-07 Last updated: 2017-12-13
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