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Tetratricopeptide repeat protein Pyg7 is essential for photosystem I assembly by interacting with PsaC in Arabidopsis
Author(s) -
Yang Huixia,
Li Pin,
Zhang Aihong,
Wen Xiaogang,
Zhang Lixin,
Lu Congming
Publication year - 2017
Publication title -
the plant journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.058
H-Index - 269
eISSN - 1365-313X
pISSN - 0960-7412
DOI - 10.1111/tpj.13618
Subject(s) - tetratricopeptide , photosystem i , arabidopsis , protein subunit , biogenesis , mutant , chemistry , rna , biology , microbiology and biotechnology , photosystem ii , biophysics , biochemistry , photosynthesis , gene
Summary Although progress has been made in determining the structure and understanding the function of photosystem I ( PSI ), the PSI assembly process remains poorly understood. PsaC is an essential subunit of PSI and participates in the transfer of electrons to ferredoxin. However, how PsaC is assembled during accumulation of the PSI complex is unknown. In the present study, we showed that Pyg7 localized to the stromal thylakoid and associated with the PSI complex. We also showed that Pyg7 interacted with PsaC. Furthermore, we found that the PSI assembly process was blocked following formation of the Psa AB heterodimer in the pyg7 mutant. In addition, the analyses of PSI stability in Pyg7 RNA i plants showed that Pyg7 is involved in maintaining the assembled PSI complex under excess‐light conditions. Moreover, we demonstrated that decreased Pyg7 content resulted in decreased efficiency of PSI assembly in Pyg7 RNA i plants. These findings suggest that the role of Pyg7 in PSI biogenesis has evolved as an essential assembly factor by interacting with PsaC in Arabidopsis , in addition to being a stability factor for PSI as seen in Synechocystis .