Structure of Psb29/Thf1 and its association with the FtsH protease complex involved in photosystem II repair in cyanobacteria.
Structure of Psb29/Thf1 and its association with the FtsH protease complex involved in photosystem II repair in cyanobacteria.
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PSB29/THF1的结构及其与蓝细菌中光系统II修复的FTSH蛋白酶复合物的关联。
DOI:
10.1098/rstb.2016.0394
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发表时间:
2017-09-26
期刊:
影响因子:
--
通讯作者:
Nixon PJ
中科院分区:
文献类型:
--
作者:
Bec Ková M;Yu J;Krynická V;Kozlo A;Shao S;Koník P;Komenda J;Murray JW;Nixon PJ
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. This article is part of the themed issue ‘Enhancing photosynthesis in crop plants: targets for improvement’.
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影响因子:
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作者:
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DOI:
10.1107/s0907444909042073
发表时间:
2010-01
期刊:
Acta crystallographica. Section D, Biological crystallography
影响因子:
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通讯作者:
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