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Psb35 Protein Stabilizes the CP47 Assembly Module and Associated High-Light Inducible Proteins during the Biogenesis of Photosystem II in the Cyanobacterium Synechocystis sp. PCC6803

SYSNO ASEP	0543368
Document Type	J - Journal Article
R&D Document Type	Journal Article
Subsidiary J	Článek ve WOS
Title	Psb35 Protein Stabilizes the CP47 Assembly Module and Associated High-Light Inducible Proteins during the Biogenesis of Photosystem II in the Cyanobacterium Synechocystis sp. PCC6803
Author(s)	Pascual-Aznar, Guillem (MBU-M) Konert, Grzegorz (MBU-M)_ORCID Bečková, Martina (MBU-M)_RID Kotabová, Eva (MBU-M)_{RID, ORCID} Gardian, Zdenko (BC-A)_RID Knoppová, Jana (MBU-M)_RID Bučinská, Lenka (MBU-M)_RID Kaňa, Radek (MBU-M)_{RID, ORCID} Sobotka, Roman (MBU-M)_{RID, ORCID} Komenda, Josef (MBU-M)_{RID, ORCID}
Source Title	Plant and Cell Physiology. - : Oxford University Press - ISSN 0032-0781 Roč. 62, č. 1 (2021), s. 178-190
Number of pages	13 s.
Language	eng - English
Country	GB - United Kingdom
Keywords	CP47 Antenna ; High-light-inducible Proteins ; Photosystem II
Subject RIV	EF - Botanics
OECD category	Plant sciences, botany
Subject RIV - cooperation	Biology Centre (since 2006) - Microbiology, Virology
R&D Projects	GX19-29225X GA ČR - Czech Science Foundation (CSF)
Method of publishing	Open access
Institutional support	MBU-M - RVO:61388971 ; BC-A - RVO:60077344
UT WOS	000642329100016
EID SCOPUS	85103607528
DOI	10.1093/pcp/pcaa148
Annotation	Photosystem II (PSII) is a large membrane protein complex performing primary charge separation in oxygenic photosynthesis. The biogenesis of PSII is a complicated process that involves a coordinated linking of assembly modules in a precise order. Each such module consists of one large chlorophyll (Chl)-binding protein, number of small membrane polypeptides, pigments and other cofactors. We isolated the CP47 antenna module from the cyanobacterium Synechocystis sp. PCC 6803 and found that it contains a 11-kDa protein encoded by the ssl2148 gene. This protein was named Psb35 and its presence in the CP47 module was confirmed by the isolation of FLAG-tagged version of Psb35. Using this pulldown assay, we showed that the Psb35 remains attached to CP47 after the integration of CP47 into PSII complexes. However, the isolated Psb35-PSIIs were enriched with auxiliary PSII assembly factors like Psb27, Psb28-1, Psb28-2 and RubA while they lacked the lumenal proteins stabilizing the PSII oxygen-evolving complex. In addition, the Psb35 co-purified with a large unique complex of CP47 and photosystem I trimer. The absence of Psb35 led to a lower accumulation and decreased stability of the CP47 antenna module and associated high-light-inducible proteins but did not change the growth rate of the cyanobacterium under the variety of light regimes. Nevertheless, in comparison with WT, the Psb35-less mutant showed an accelerated pigment bleaching during prolonged dark incubation. The results suggest an involvement of Psb35 in the life cycle of cyanobacterial Chl-binding proteins, especially CP47.
Workplace	Institute of Microbiology
Contact	Eliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231
Year of Publishing	2022
Electronic address	https://academic.oup.com/pcp/article/62/1/178/6015241?login=true

Number of the records: 1