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A change in the sensitivity of elongation factor G to oxidation protects photosystem II from photoinhibition in Synechocystis sp. PCC 6803
Author(s) -
Ejima Kayoko,
Kawaharada Tomoko,
Inoue Shuhei,
Kojima Kouji,
Nishiyama Yoshitaka
Publication year - 2012
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2012.01.042
Subject(s) - photoinhibition , photosystem ii , synechocystis , chemistry , cysteine , biochemistry , elongation factor , photosystem i , biophysics , oxidative stress , serine , photosynthesis , biology , enzyme , mutant , rna , gene , ribosome
The repair of photosystem II (PSII) after photodamage is particularly sensitive to oxidative stress and inhibition of such repair is associated with the oxidation of specific cysteine residues in elongation factor G (EF‐G), a key translation factor, in the cyanobacterium Synechocystis sp. PCC 6803. Expression of mutated EF‐G with a target cysteine residue replaced by serine in Synechocystis resulted in the protection of PSII from photoinhibition. This protection was attributable to the enhanced repair of PSII via acceleration of the synthesis of the D1 protein, which might have been due to reduced sensitivity of protein synthesis to oxidative stress.