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Photosystem II protein 33, a protein conserved in the plastid lineage, is associated with the chloroplast thylakoid membrane and provides stability to photosystem II supercomplexes in Arabidopsis
Uppsala University, Disciplinary Domain of Science and Technology, Chemistry, Department of Chemistry - Ångström, Molecular Biomimetics.
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2015 (English)In: Plant Physiology, ISSN 0032-0889, E-ISSN 1532-2548, Vol. 167, no 2, 481-492 p.Article in journal (Refereed) Published
Abstract [en]

Photosystem II (PSII) is a multiprotein complex that catalyzes the light-driven water-splitting reactions of oxygenic photosynthesis. Light absorption by PSII leads to the production of excited states and reactive oxygen species that can cause damage to this complex. Here, we describe Arabidopsis (Arabidopsis thaliana) At1g71500, which encodes a previously uncharacterized protein that is a PSII auxiliary core protein and hence is named PHOTOSYSTEM II PROTEIN33 (PSB33). We present evidence that PSB33 functions in the maintenance of PSII-light-harvesting complex II (LHCII) supercomplex organization. PSB33 encodes a protein with a chloroplast transit peptide and one transmembrane segment. In silico analysis of PSB33 revealed a light-harvesting complex-binding motif within the transmembrane segment and a large surface-exposed head domain. Biochemical analysis of PSII complexes further indicates that PSB33 is an integral membrane protein located in the vicinity of LHCII and the PSII CP43 reaction center protein. Phenotypic characterization of mutants lacking PSB33 revealed reduced amounts of PSII-LHCII supercomplexes, very low state transition, and a lower capacity for nonphotochemical quenching, leading to increased photosensitivity in the mutant plants under light stress. Taken together, these results suggest a role for PSB33 in regulating and optimizing photosynthesis in response to changing light levels.

Place, publisher, year, edition, pages
2015. Vol. 167, no 2, 481-492 p.
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Biochemistry and Molecular Biology
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URN: urn:nbn:se:uu:diva-240043DOI: 10.​1104/​pp.​114.​253336ISI: 000348652700014PubMedID: 25511433OAI: oai:DiVA.org:uu-240043DiVA: diva2:775817
Available from: 2015-01-05 Created: 2015-01-05 Last updated: 2016-02-23Bibliographically approved

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Mamedov, Fikret
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