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

DOI: 10.1098/rstb.2016.0394 DOI Help

Authors: Martina Bec̆ková (University of South Bohemia) , Jianfeng Yu (Imperial College London) , Vendula Krynická (Institute of Microbiology, Center Algatech) , Amanda Kozlo (Imperial College London) , Shengxi Shao (Imperial College London) , Peter Koník (University of South Bohemia) , Josef Komenda (University of South Bohemia) , James W. Murray (Imperial College London) , Peter J. Nixon (University of South Bohemia)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Philosophical Transactions Of The Royal Society B: Biological Sciences , VOL 372

State: Published (Approved)
Published: August 2017
Diamond Proposal Number(s): 7299

Open Access Open Access

Abstract: 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.

Journal Keywords: photoinhibition; thylakoid formation 1 gene; D1 subunit; Synechocystis; thylakoid membrane; hypersensitive response

Diamond Keywords: Cyanobacteria; Photosynthesis

Subject Areas: Biology and Bio-materials

Instruments: I04-1-Macromolecular Crystallography (fixed wavelength)

Added On: 23/08/2017 09:05


Discipline Tags:

Plant science Structural biology Biophysics Life Sciences & Biotech

Technical Tags:

Diffraction Macromolecular Crystallography (MX)