Počet záznamů: 1
Structure of Psb29/Thf1 and its association with the FtsH protease complex involved in photosystem II repair in cyanobacteria
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SYSNO ASEP 0484710 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název Structure of Psb29/Thf1 and its association with the FtsH protease complex involved in photosystem II repair in cyanobacteria Tvůrce(i) Bečková, Martina (MBU-M) RID
Yu, J.F. (GB)
Krynická, Vendula (MBU-M) RID
Kozlo, A. (GB)
Shao, S.X. (GB)
Koník, Peter (MBU-M)
Komenda, Josef (MBU-M) RID, ORCID
Murray, J. W. (GB)
Nixon, P. J. (GB)Číslo článku 20160394 Zdroj.dok. Philosophical Transactions of the Royal Society B-Biological Sciences. - : Royal Society Publishing - ISSN 0962-8436
Roč. 372, č. 1730 (2017)Poč.str. 10 s. Jazyk dok. eng - angličtina Země vyd. GB - Velká Británie Klíč. slova photoinhibition ; thylakoid formation 1 gene ; D1 subunit Vědní obor RIV EE - Mikrobiologie, virologie Obor OECD Microbiology CEP GBP501/12/G055 GA ČR - Grantová agentura ČR LO1416 GA MŠMT - Ministerstvo školství, mládeže a tělovýchovy ED2.1.00/19.0392 GA MŠMT - Ministerstvo školství, mládeže a tělovýchovy Institucionální podpora MBU-M - RVO:61388971 UT WOS 000407717300014 EID SCOPUS 85027545467 DOI 10.1098/rstb.2016.0394 Anotace One strategy for enhancing photosynthesis in crop plants is to improve their ability to repair photosystem II (PSII) in response to irreversible damage by light. Despite the pivotal role of thylakoid-embedded FtsH protease complexes in the selective degradation of PSII subunits during repair, little is known about the factors involved in regulating FtsH expression. Here we show using the cyanobacterium Synechocystis sp. PCC 6803 that the Psb29 subunit, originally identified as a minor component of His-tagged PSII preparations, physically interacts with FtsH complexes in vivo and is required for normal accumulation of the FtsH2/FtsH3 hetero-oligomeric complex involved in PSII repair. We show using X-ray crystallography that Psb29 from Thermosynechococcus elongatus has a unique fold consisting of a helical bundle and an extended C-terminal helix and contains a highly conserved region that might be involved in binding to FtsH. A similar interaction is likely to occur in Arabidopsis chloroplasts between the Psb29 homologue, termed THF1, and the FTSH2/FTSH5 complex. The direct involvement of Psb29/THF1 in FtsH accumulation helps explain why THF1 is a target during the hypersensitive response in plants induced by pathogen infection. Downregulating FtsH function and the PSII repair cycle via THF1 would contribute to the production of reactive oxygen species, the loss of chloroplast function and cell death. Pracoviště Mikrobiologický ústav Kontakt Eliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231 Rok sběru 2018
Počet záznamů: 1