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Schröder, Wolfgang P.ORCID iD iconorcid.org/0000-0002-9492-5113
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Publications (10 of 57) Show all publications
Chen, Y.-E., Yuan, S., Lezhneva, L., Meurer, J., Schwenkert, S., Mamedov, F. & Schröder, W. P. (2019). The Low Molecular Mass Photosystem II Protein PsbTn is Important for Light Acclimation. Plant Physiology, 179(4), 1739-1753
Open this publication in new window or tab >>The Low Molecular Mass Photosystem II Protein PsbTn is Important for Light Acclimation
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2019 (English)In: Plant Physiology, ISSN 0032-0889, E-ISSN 1532-2548, Vol. 179, no 4, p. 1739-1753Article in journal (Refereed) Published
Abstract [en]

Photosystem II (PSII) is a supramolecular complex containing over 30 protein subunits and a large set of cofactors including various pigments and quinones as well as Mn, Ca, Cl, and Fe ions. Eukaryotic PSII complexes contain many subunits not found in their bacterial counterparts, including the proteins PsbP, PsbQ, PsbS, and PsbW, as well as the highly homologous, low molecular mass subunits PsbTn1 and PsbTn2 whose function is currently unknown. To determine the function of PsbTn1 and PsbTn2, we generated single and double psbTn1 and psbTn2 knock-out mutants in Arabidopsis thaliana. Cross-linking and reciprocal co-immunoprecipitation experiments revealed that PsbTn is a lumenal PSII protein situated next to the cytochrome b559 subunit PsbE. The removal of the PsbTn proteins decreased the oxygen evolution rate and PSII core phosphorylation level but increased the susceptibility of PSII to photoinhibition and the production of reactive oxygen species. The assembly and stability of PSII were unaffected, indicating that the deficiencies of the psbTn1 psbTn2 double mutants are due to structural changes. Double mutants exhibited a higher rate of non-photochemical quenching of excited states than the wild type and single mutants, as well as slower state transition kinetics and a lower quantum yield of PSII when grown in the field. Based on these results, we propose that the main function of the PsbTn proteins is to enable PSII to acclimate to light shifts or intense illumination.

Place, publisher, year, edition, pages
Rockville: American Society of Plant Biologists, 2019
National Category
Biochemistry and Molecular Biology
Identifiers
urn:nbn:se:umu:diva-156389 (URN)10.1104/pp.18.01251 (DOI)000462993100045 ()30538167 (PubMedID)
Funder
Carl Tryggers foundation
Note

Short title: PsbTn protein regulates light adaptation

Available from: 2019-02-14 Created: 2019-02-14 Last updated: 2019-05-23Bibliographically approved
Dubreuil, C., Jin, X., Barajas-López, J. d., Hewitt, T. C., Tanz, S. K., Dobrenel, T., . . . Strand, Å. (2018). Establishment of Photosynthesis through Chloroplast Development Is Controlled by Two Distinct Regulatory Phases. Plant Physiology, 176(2), 1199-1214
Open this publication in new window or tab >>Establishment of Photosynthesis through Chloroplast Development Is Controlled by Two Distinct Regulatory Phases
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2018 (English)In: Plant Physiology, ISSN 0032-0889, E-ISSN 1532-2548, Vol. 176, no 2, p. 1199-1214Article in journal (Refereed) Published
Abstract [en]

Chloroplasts develop from undifferentiated proplastids present in meristematic tissue. Thus, chloroplast biogenesis is closely connected to leaf development, which restricts our ability to study the process of chloroplast biogenesis per se. As a consequence, we know relatively little about the regulatory mechanisms behind the establishment of the photosynthetic reactions and how the activities of the two genomes involved are coordinated during chloroplast development. We developed a single cell-based experimental system from Arabidopsis (Arabidopsis thaliana) with high temporal resolution allowing for investigations of the transition from proplastids to functional chloroplasts. Using this unique cell line, we could show that the establishment of photosynthesis is dependent on a regulatory mechanism involving two distinct phases. The first phase is triggered by rapid light-induced changes in gene expression and the metabolome. The second phase is dependent on the activation of the chloroplast and generates massive changes in the nuclear gene expression required for the transition to photosynthetically functional chloroplasts. The second phase also is associated with a spatial transition of the chloroplasts from clusters around the nucleus to the final position at the cell cortex. Thus, the establishment of photosynthesis is a two-phase process with a clear checkpoint associated with the second regulatory phase allowing coordination of the activities of the nuclear and plastid genomes.

Place, publisher, year, edition, pages
American Society of Plant Biologists, 2018
National Category
Botany
Identifiers
urn:nbn:se:umu:diva-140157 (URN)10.1104/pp.17.00435 (DOI)000424285500021 ()28626007 (PubMedID)
Projects
Bio4Energy
Available from: 2017-10-02 Created: 2017-10-02 Last updated: 2019-08-30Bibliographically approved
Shevela, D., Schröder, W. P. & Messinger, J. (2018). Liquid-phase measurements of photosynthetic oxygen evolution. Methods in Molecular Biology, 1770, 197-211
Open this publication in new window or tab >>Liquid-phase measurements of photosynthetic oxygen evolution
2018 (English)In: Methods in Molecular Biology, ISSN 1064-3745, E-ISSN 1940-6029, Vol. 1770, p. 197-211Article in journal (Refereed) Published
Abstract [en]

This chapter compares two different techniques for monitoring photosynthetic O2 production: the widespread Clark-type O2 electrode and the more sophisticated membrane inlet mass spectrometry (MIMS) technique. We describe how a simple membrane inlet for MIMS can be made out of a commercial Clark-type cell, and outline the advantages and drawbacks of the two techniques to guide researchers in deciding which method to use. Protocols and examples are given for measuring O2 evolution rates and for determining the number of chlorophyll molecules per active photosystem II reaction center.

Keywords
Photosynthetic water oxidation, O2 evolution, Photosystem II, Clark-type electrode, Membrane inlet mass spectrometry
National Category
Biophysics
Identifiers
urn:nbn:se:umu:diva-152593 (URN)10.1007/978-1-4939-7786-4_11 (DOI)29978403 (PubMedID)
Available from: 2018-10-15 Created: 2018-10-15 Last updated: 2018-11-09Bibliographically approved
Mishra, Y., Hall, M., Locmelis, R., Nam, K., Söderberg, C. A. G., Storm, P., . . . Sauer, U. H. (2017). Active-site plasticity revealed in the asymmetric dimer of AnPrx6 the 1-Cys peroxiredoxin and molecular chaperone from Anabaena sp. PCC 7120. Scientific Reports, 7, Article ID 17151.
Open this publication in new window or tab >>Active-site plasticity revealed in the asymmetric dimer of AnPrx6 the 1-Cys peroxiredoxin and molecular chaperone from Anabaena sp. PCC 7120
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2017 (English)In: Scientific Reports, ISSN 2045-2322, E-ISSN 2045-2322, Vol. 7, article id 17151Article in journal (Refereed) Published
Abstract [en]

Peroxiredoxins (Prxs) are vital regulators of intracellular reactive oxygen species levels in all living organisms. Their activity depends on one or two catalytically active cysteine residues, the peroxidatic Cys (C-P) and, if present, the resolving Cys (C-R). A detailed catalytic cycle has been derived for typical 2-Cys Prxs, however, little is known about the catalytic cycle of 1-Cys Prxs. We have characterized Prx6 from the cyanobacterium Anabaena sp. strain PCC7120 (AnPrx6) and found that in addition to the expected peroxidase activity, AnPrx6 can act as a molecular chaperone in its dimeric state, contrary to other Prxs. The AnPrx6 crystal structure at 2.3 angstrom resolution reveals different active site conformations in each monomer of the asymmetric obligate homo-dimer. Molecular dynamic simulations support the observed structural plasticity. A FSH motif, conserved in 1-Cys Prxs, precedes the active site PxxxTxxCp signature and might contribute to the 1-Cys Prx reaction cycle.

Place, publisher, year, edition, pages
Nature Publishing Group, 2017
National Category
Structural Biology
Identifiers
urn:nbn:se:umu:diva-143523 (URN)10.1038/s41598-017-17044-3 (DOI)000417354200004 ()29215017 (PubMedID)2-s2.0-85038074530 (Scopus ID)
Note

The original version of this Article contained an error in the title of the paper, where “Anabaena sp. PCC 7120” was incorrectly given as “Anabaena sp. PCC 7210”. This has now been corrected in the PDF and HTML versions of the Article, and in the accompanying Supplementary Information file.

Errata: Author Correction: Active-site plasticity revealed in the asymmetric dimer of AnPrx6 the 1-Cys peroxiredoxin and molecular chaperone from Anabaena sp. PCC 7120. Scientifc reports. 2018;8:8658. DOI: 10.1038/s41598-018-26715-8

Available from: 2018-01-04 Created: 2018-01-04 Last updated: 2018-06-15Bibliographically approved
Chen, Y.-E., Yuan, S. & Schröder, W. P. (2016). Comparison of methods for extracting thylakoid membranes of Arabidopsis plants. Physiologia Plantarum: An International Journal for Plant Biology, 156(1), 3-12
Open this publication in new window or tab >>Comparison of methods for extracting thylakoid membranes of Arabidopsis plants
2016 (English)In: Physiologia Plantarum: An International Journal for Plant Biology, ISSN 0031-9317, E-ISSN 1399-3054, Vol. 156, no 1, p. 3-12Article in journal (Refereed) Published
Abstract [en]

Robust and reproducible methods for extracting thylakoid membranes are required for the analysis of photosynthetic processes in higher plants such as Arabidopsis. Here, we compare three methods for thylakoid extraction using two different buffers. Method I involves homogenizing the plant material witha metal/glass blender; method II involves manually grinding the plant materialin ice-cold grinding buffer with a mortar and method III entails snap-freezing followed by manual grinding with a mortar, after which the frozen powder is thawed in isolation buffer. Thylakoid membrane samples extracted using each method were analyzed with respect to protein and chlorophyll content, yields relative to starting material, oxygen-evolving activity, protein complex content and phosphorylation. We also examined how the use of fresh and frozen thylakoid material affected the extracts’ contents of protein complexes. The use of different extraction buffers did not significantly alter the protein contentof the extracts in any case. Method I yielded thylakoid membranes with the highest purity and oxygen-evolving activity. Method III used low amounts of starting material and was capable of capturing rapid phosphorylation changes in the sample at the cost of higher levels of contamination. Method II yielded thylakoid membrane extracts with properties intermediate between those obtained with the other two methods. Finally, frozen and freshly isolated thylakoid membranes performed identically in blue native-polyacrylamide gel electrophoresis experiments conducted in order to separate multimeric protein supracomplexes.

Keywords
BN-PAGE, blue native-polyacrylamide gel electrophoresis, Chl, chlorophyll, COXII, cytochrome oxidase subunit II, LHC, light-harvesting complex, PS, photosystem, SDS, sodium dodecyl sulfate
National Category
Analytical Chemistry Plant Biotechnology
Identifiers
urn:nbn:se:umu:diva-110442 (URN)10.1111/ppl.12384 (DOI)000367687800002 ()26337850 (PubMedID)
Available from: 2015-10-21 Created: 2015-10-21 Last updated: 2018-06-07Bibliographically approved
Toth, T. N., Rai, N., Solymosi, K., Zsiros, O., Schröder, W. P., Garab, G., . . . Kovacs, L. (2016). Fingerprinting the macro-organisation of pigment-protein complexes in plant thylakoid membranes in vivo by circular-dichroism spectroscopy. Biochimica et Biophysica Acta - Bioenergetics, 1857(9), 1479-1489
Open this publication in new window or tab >>Fingerprinting the macro-organisation of pigment-protein complexes in plant thylakoid membranes in vivo by circular-dichroism spectroscopy
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2016 (English)In: Biochimica et Biophysica Acta - Bioenergetics, ISSN 0005-2728, E-ISSN 1879-2650, Vol. 1857, no 9, p. 1479-1489Article in journal (Refereed) Published
Abstract [en]

Macro-organisation of the protein complexes in plant thylakoid membranes plays important roles in the regulation and fine-tuning of photosynthetic activity. These delicate structures might, however, undergo substantial changes during isolating the thylakoid membranes or during sample preparations, e.g., for electron microscopy. Circular-dichroism (CD) spectroscopy is a non-invasive technique which can thus be used on intact samples. Via excitonic and psi-type CD bands, respectively, it carries information on short-range excitonic pigment-pigment interactions and the macro-organisation (chiral macrodomains) of pigment-protein complexes (psi, polymer or salt-induced). In order to obtain more specific information on the origin of the major psi-type CD bands, at around (+)506, (-)674 and (+)690 nm, we fingerprinted detached leaves and isolated thylakoid membranes of wild-type and mutant plants and also tested the effects of different environmental conditions in vivo. We show that (i) the chiral macrodomains disassemble upon mild detergent treatments, but not after crosslinking the protein complexes; (ii) in different wild-type leaves of dicotyledonous and monocotyledonous angiosperms the CD features are quite robust, displaying very similar excitonic and psi-type bands, suggesting similar protein composition and (macro-) organisation of photosystem II (PSII) supercomplexes in the grana; (iii) the main positive psi-type bands depend on light-harvesting protein II contents of the membranes; (iv) the (+)506 nm band appears only in the presence of PSII-LHCII supercomplexes and does not depend on the xanthophyll composition of the membranes. Hence, CD spectroscopy can be used to detect different macro-domains in the thylakoid membranes with different outer antenna compositions in vivo. 

Keywords
Circular dichroism, Chiral macrodomain, Light-harvesting complexes, Photosystem II supercomplexes, i-type CD, Thylakoid membrane, METER S, 1976, BIOCHEMICAL JOURNAL, V156, P469 Bianchi Silvia, 2011, PLANT CELL, V23, P2659
National Category
Biochemistry and Molecular Biology
Identifiers
urn:nbn:se:umu:diva-126321 (URN)10.1016/j.bbabio.2016.04.287 (DOI)000382590400014 ()27154055 (PubMedID)
Available from: 2016-11-02 Created: 2016-10-03 Last updated: 2018-06-09Bibliographically approved
Plöchinger, M., Schwenkert, S., von Sydow, L., Schröder, W. P. & Meurer, J. (2016). Functional Update of the Auxiliary Proteins PsbW, PsbY, HCF136, PsbN, TerC and ALB3 in Maintenance and Assembly of PSII. Frontiers in Plant Science, 7, Article ID 423.
Open this publication in new window or tab >>Functional Update of the Auxiliary Proteins PsbW, PsbY, HCF136, PsbN, TerC and ALB3 in Maintenance and Assembly of PSII
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2016 (English)In: Frontiers in Plant Science, ISSN 1664-462X, E-ISSN 1664-462X, Vol. 7, article id 423Article in journal (Refereed) Published
Abstract [en]

Assembly of Photosystem (PS) II in plants has turned out to be a highly complex process which, at least in part, occurs in a sequential order and requires many more auxiliary proteins than subunits present in the complex. Owing to the high evolutionary conservation of the subunit composition and the three-dimensional structure of the PSII complex, most plant factors involved in the biogenesis of PSII originated from cyanobacteria and only rarely evolved de novo. Furthermore, in chloroplasts the initial assembly steps occur in the non-appressed stroma lamellae, whereas the final assembly including the attachment of the major LHCII antenna proteins takes place in the grana regions. The stroma lamellae are also the place where part of PSII repair occurs, which very likely also involves assembly factors. In cyanobacteria initial PSII assembly also occurs in the thylakoid membrane, in so-called thylakoid centers, which are in contact with the plasma membrane. Here, we provide an update on the structures, localisations, topologies, functions, expression and interactions of the low molecular mass PSII subunits PsbY, PsbW and the auxiliary factors HCF136, PsbN, TerC and ALB3, assisting in PSII complex assembly and protein insertion into the thylakoid membrane.

Keywords
PSII photosystem II, cytochrome b559, assembly, low molecular mass proteins, Arabidopsis
National Category
Biochemistry and Molecular Biology
Identifiers
urn:nbn:se:umu:diva-120622 (URN)10.3389/fpls.2016.00423 (DOI)000373599400001 ()27092151 (PubMedID)
Available from: 2016-08-16 Created: 2016-05-18 Last updated: 2018-06-07Bibliographically approved
von Sydow, L., Schwenkert, S., Meurer, J., Funk, C., Mamedov, F. & Schröder, W. P. (2016). The PsbY protein of Arabidopsis Photosystem II is important for the redox control of cytochrome b559. Biochimica et Biophysica Acta - Bioenergetics, 1857(9), 1524-1533
Open this publication in new window or tab >>The PsbY protein of Arabidopsis Photosystem II is important for the redox control of cytochrome b559
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2016 (English)In: Biochimica et Biophysica Acta - Bioenergetics, ISSN 0005-2728, E-ISSN 1879-2650, Vol. 1857, no 9, p. 1524-1533Article in journal (Refereed) Published
Abstract [en]

Abstract Photosystem II is a protein complex embedded in the thylakoid membrane of photosynthetic organisms and performs the light driven water oxidation into electrons and molecular oxygen that initiate the photosynthetic process. This important complex is composed of more than two dozen of intrinsic and peripheral subunits, of those half are low molecular mass proteins. PsbY is one of those low molecular mass proteins; this 4.7–4.9 kDa intrinsic protein seems not to bind any cofactors. Based on structural data from cyanobacterial and red algal Photosystem II PsbY is located closely or in direct contact with cytochrome b559. Cytb559 consists of two protein subunits (PsbE and PsbF) ligating a heme-group in-between them. While the exact function of this component in Photosystem II has not yet been clarified, a crucial role for assembly and photo-protection in prokaryotic complexes has been suggested. One unique feature of Cytb559 is its redox-heterogeneity, forming high, medium and low potential, however, neither origin nor mechanism are known. To reveal the function of PsbY within Photosystem II of Arabidopsis we have analysed PsbY knock-out plants and compared them to wild type and to complemented mutant lines. We show that in the absence of PsbY protein Cytb559 is only present in its oxidized, low potential form and plants depleted of PsbY were found to be more susceptible to photoinhibition.

Keywords
Photosystem II, Thylakoid membrane, PsbY protein, Cytochrome b559
National Category
Biochemistry and Molecular Biology
Identifiers
urn:nbn:se:umu:diva-124444 (URN)10.1016/j.bbabio.2016.05.004 (DOI)000382590400019 ()27220875 (PubMedID)
Available from: 2016-08-11 Created: 2016-08-11 Last updated: 2018-06-07Bibliographically approved
Uberegui, E., Hall, M., Lorenzo, O., Schröder, W. P. & Balsera, M. (2015). An Arabidopsis soluble chloroplast proteomic analysis reveals the participation of the Executer pathway in response to increased light conditions. Journal of Experimental Botany, 66(7), 2067-2077
Open this publication in new window or tab >>An Arabidopsis soluble chloroplast proteomic analysis reveals the participation of the Executer pathway in response to increased light conditions
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2015 (English)In: Journal of Experimental Botany, ISSN 0022-0957, E-ISSN 1460-2431, Vol. 66, no 7, p. 2067-2077Article in journal (Refereed) Published
Abstract [en]

The Executer1 and Executer2 proteins have a fundamental role in the signalling pathway mediated by singlet oxygen in chloroplast; nonetheless, not much is known yet about their specific activity and features. Herein, we have followed a differential-expression proteomics approach to analyse the impact of Executer on the soluble chloroplast protein abundance in Arabidopsis. Because singlet oxygen plays a significant role in signalling the oxidative response of plants to light, our analysis also included the soluble chloroplast proteome of plants exposed to a moderate light intensity in the time frame of hours. A number of light- and genotype-responsive proteins were detected, and mass-spectrometry identification showed changes in abundance of several photosynthesis-and carbon metabolism-related proteins as well as proteins involved in plastid mRNA processing. Our results support the participation of the Executer proteins in signalling and control of chloroplast metabolism, and in the regulation of plant response to environmental changes.

Keywords
Abiotic stress, acclimation response, chloroplast metabolism, DIGE, light, retrograde signalling, ROS
National Category
Biological Sciences
Identifiers
urn:nbn:se:umu:diva-106375 (URN)10.1093/jxb/erv018 (DOI)000353894100029 ()25740923 (PubMedID)
Available from: 2015-07-15 Created: 2015-07-14 Last updated: 2018-06-07Bibliographically approved
Strimbeck, G. R., Schaberg, P. G., Fossdal, C. G., Schröder, W. P. & Kjellsen, T. D. (2015). Extreme low temperature tolerance in woody plants. Frontiers in Plant Science, 6, Article ID 884.
Open this publication in new window or tab >>Extreme low temperature tolerance in woody plants
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2015 (English)In: Frontiers in Plant Science, ISSN 1664-462X, E-ISSN 1664-462X, Vol. 6, article id 884Article, review/survey (Refereed) Published
Abstract [en]

Woody plants in boreal to arctic environments and high mountains survive prolonged exposure to temperatures below -40°C and minimum temperatures below -60°C, and laboratory tests show that many of these species can also survive immersion in liquid nitrogen at -196°C. Studies of biochemical changes that occur during acclimation, including recent proteomic and metabolomic studies, have identified changes in carbohydrate and compatible solute concentrations, membrane lipid composition, and proteins, notably dehydrins, that may have important roles in survival at extreme low temperature (ELT). Consideration of the biophysical mechanisms of membrane stress and strain lead to the following hypotheses for cellular and molecular mechanisms of survival at ELT: (1) Changes in lipid composition stabilize membranes at temperatures above the lipid phase transition temperature (-20 to -30°C), preventing phase changes that result in irreversible injury. (2) High concentrations of oligosaccharides promote vitrification or high viscosity in the cytoplasm in freeze-dehydrated cells, which would prevent deleterious interactions between membranes. (3) Dehydrins bind membranes and further promote vitrification or act stearically to prevent membrane–membrane interactions.

Place, publisher, year, edition, pages
Frontiers Media, 2015
Keywords
cold, frost, tolerance, hardiness, acclimation, hardening, biochemistry, vitirification
National Category
Chemical Sciences
Identifiers
urn:nbn:se:umu:diva-110404 (URN)10.3389/fpls.2015.00884 (DOI)000364344800001 ()26539202 (PubMedID)
Available from: 2015-10-21 Created: 2015-10-21 Last updated: 2018-06-07Bibliographically approved
Projects
Regulatory roles of small, nuclear-encoded proteins in the organisation of macro-complexes in photosynthetic membranes [2008-03207_VR]; Umeå University
Organisations
Identifiers
ORCID iD: ORCID iD iconorcid.org/0000-0002-9492-5113

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