A change in the sensitivity of elongation factor G to oxidation protects photosystem II from photoinhibition in Synechocystis sp. PCC 6803.
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.
Department of Biochemistry and Molecular Biology, Graduate School of Science and Engineering, Saitama University, Sakura-ku, Saitama, Japan.
Kayoko
K
Ejima
Tomoko
T
Kawaharada
Shuhei
S
Inoue
Kouji
K
Kojima
Yoshitaka
Y
Nishiyama
D008027:Light; D016297:Mutagenesis, Site-Directed; D010084:Oxidation-Reduction; D018384:Oxidative Stress; D020653:Peptide Elongation Factor G / Q000235:genetics / Q000378:metabolism*; D045332:Photosystem II Protein Complex / Q000502:physiology*; D014176:Protein Biosynthesis; D017382:Reactive Oxygen Species / Q000378:metabolism; D046939:Synechocystis / Q000378:metabolism*
D020653:Peptide Elongation Factor G; D045332:Photosystem II Protein Complex; D017382:Reactive Oxygen Species