Number of the records: 1  

Structure of Psb29/Thf1 and its association with the FtsH protease complex involved in photosystem II repair in cyanobacteria

  1. 1.
    0484710 - MBÚ 2018 RIV GB eng J - Journal Article
    Bečková, Martina - Yu, J.F. - Krynická, Vendula - Kozlo, A. - Shao, S.X. - Koník, Peter - Komenda, Josef - Murray, J. W. - Nixon, P. J.
    Structure of Psb29/Thf1 and its association with the FtsH protease complex involved in photosystem II repair in cyanobacteria.
    Philosophical Transactions of the Royal Society B-Biological Sciences. Roč. 372, č. 1730 (2017), č. článku 20160394. ISSN 0962-8436. E-ISSN 1471-2970
    R&D Projects: GA ČR GBP501/12/G055; GA MŠMT(CZ) LO1416; GA MŠMT(CZ) ED2.1.00/19.0392
    Institutional support: RVO:61388971
    Keywords : photoinhibition * thylakoid formation 1 gene * D1 subunit
    OECD category: Microbiology
    Impact factor: 5.666, year: 2017

    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.
    Permanent Link: http://hdl.handle.net/11104/0280078

     
    FileDownloadSizeCommentaryVersionAccess
    131_Structure of Psb29Thf1 and its association.pdf61.1 MBPublisher’s postprintrequire
     
Number of the records: 1  

  This site uses cookies to make them easier to browse. Learn more about how we use cookies.