Počet záznamů: 1
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
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SYSNO ASEP 0543368 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název 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 Tvůrce(i) Pascual-Aznar, Guillem (MBU-M)
Konert, Grzegorz (MBU-M) ORCID
Bečková, Martina (MBU-M) RID, ORCID
Kotabová, Eva (MBU-M) RID, ORCID
Gardian, Zdenko (BC-A) RID
Knoppová, Jana (MBU-M) RID, ORCID
Bučinská, Lenka (MBU-M) RID
Kaňa, Radek (MBU-M) RID, ORCID
Sobotka, Roman (MBU-M) RID, ORCID
Komenda, Josef (MBU-M) RID, ORCIDZdroj.dok. Plant and Cell Physiology. - : Oxford University Press - ISSN 0032-0781
Roč. 62, č. 1 (2021), s. 178-190Poč.str. 13 s. Jazyk dok. eng - angličtina Země vyd. GB - Velká Británie Klíč. slova CP47 Antenna ; High-light-inducible Proteins ; Photosystem II Vědní obor RIV EF - Botanika Obor OECD Plant sciences, botany Vědní obor RIV – spolupráce Biologické centrum (od r. 2006) - Mikrobiologie, virologie CEP GX19-29225X GA ČR - Grantová agentura ČR Způsob publikování Open access Institucionální podpora MBU-M - RVO:61388971 ; BC-A - RVO:60077344 UT WOS 000642329100016 EID SCOPUS 85103607528 DOI https://doi.org/10.1093/pcp/pcaa148 Anotace 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. Pracoviště Mikrobiologický ústav Kontakt Eliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231 Rok sběru 2022 Elektronická adresa https://academic.oup.com/pcp/article/62/1/178/6015241?login=true
Počet záznamů: 1