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Role of Novel Dimeric Photosystem II (PSII)-Psb27 Protein Complex in PSII Repair
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Photochemistry and Molecular Science, Molecular Biomimetics.
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Photochemistry and Molecular Science, Molecular Biomimetics.
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2011 (English)In: Journal of Biological Chemistry, ISSN 0021-9258, E-ISSN 1083-351X, Vol. 286, no 34, 29548-29555 p.Article in journal (Refereed) Published
Abstract [en]

The multisubunit membrane protein complex Photosystem II (PSII) catalyzes one of the key reactions in photosynthesis: the light-driven oxidation of water. Here, we focus on the role of the Psb27 assembly factor, which is involved in biogenesis and repair after light-induced damage of the complex. Weshow that Psb27 is essential for the survival of cyanobacterial cells grown under stress conditions. The combination of cold stress (30 degrees C) and high light stress (1000 mu mol of photons x m(-2) x s(-1)) led to complete inhibition of growth in a Delta psb27 mutant strain of the thermophilic cyanobacterium Thermosynechococcus elongatus, whereas wild-type cells continued to grow. Moreover, Psb27-containing PSII complexes became the predominant PSII species in preparations from wild-type cells grown under cold stress. Two different PSII-Psb27 complexes were isolated and characterized in this study. The first complex represents the known monomeric PSII-Psb27 species, which is involved in the assembly of PSII. Additionally, a novel dimeric PSII-Psb27 complex could be allocated in the repair cycle, i.e. in processes after inactivation of PSII, by (15)N pulse-label experiments followed by mass spectrometry analysis. Comparison with the corresponding PSII species from Delta psb27 mutant cells showed that Psb27 prevented the release of manganese from the previously inactivated complex. These results indicate a more complex role of the Psb27 protein within the life cycle of PSII, especially under stress conditions.

Place, publisher, year, edition, pages
2011. Vol. 286, no 34, 29548-29555 p.
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Biochemistry and Molecular Biology
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URN: urn:nbn:se:uu:diva-158305DOI: 10.1074/jbc.M111.238394ISI: 000294046600012OAI: oai:DiVA.org:uu-158305DiVA: diva2:439265
Available from: 2011-09-07 Created: 2011-09-06 Last updated: 2017-12-08Bibliographically approved

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Mamedov, FikretStyring, Stenbjörn

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