A change in the sensitivity of elongation factor G to oxidation protects photosystem II from photoinhibition in Synechocystis sp. PCC 6803

Kayoko Ejima; Tomoko Kawaharada; Shuhei Inoue; Kouji Kojima; Yoshitaka Nishiyama

doi:10.1016/j.febslet.2012.01.042

A change in the sensitivity of elongation factor G to oxidation protects photosystem II from photoinhibition in Synechocystis sp. PCC 6803

Kayoko Ejima, Tomoko Kawaharada, Shuhei Inoue, Kouji Kojima, Yoshitaka Nishiyama

ENG - Biomolecular Engineering

Research output: Contribution to journal › Article › peer-review

22 Citations (Scopus)

Abstract

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.

Original language	English
Pages (from-to)	778-783
Number of pages	6
Journal	FEBS Letters
Volume	586
Issue number	6
DOIs	https://doi.org/10.1016/j.febslet.2012.01.042
Publication status	Published - 2012 Mar 23

Keywords

Elongation factor G
Oxidative stress
Photoinhibition
Photosystem II
Protein synthesis
Repair

ASJC Scopus subject areas

Biophysics
Structural Biology
Biochemistry
Molecular Biology
Genetics
Cell Biology

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title = "A change in the sensitivity of elongation factor G to oxidation protects photosystem II from photoinhibition in Synechocystis sp. PCC 6803",

abstract = "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.",

keywords = "Elongation factor G, Oxidative stress, Photoinhibition, Photosystem II, Protein synthesis, Repair",

author = "Kayoko Ejima and Tomoko Kawaharada and Shuhei Inoue and Kouji Kojima and Yoshitaka Nishiyama",

note = "Funding Information: This work was supported, in part, by a Grant-in-Aid for Scientific Research from the Ministry of Education, Culture, Sports, Science, and Technology of Japan ( no. 21570033 to Y.N.) and by a grant from the Asahi Glass Foundation (to Y.N.). The authors thank Prof. Masahiko Ikeuchi (the University of Tokyo) for providing the pTCP2031 vector. They also thank Mr. Tomohisa Niimi (Saitama University) for radioisotope analysis. Copyright: Copyright 2012 Elsevier B.V., All rights reserved.",

year = "2012",

month = mar,

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doi = "10.1016/j.febslet.2012.01.042",

language = "English",

volume = "586",

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journal = "FEBS Letters",

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AU - Ejima, Kayoko

AU - Kawaharada, Tomoko

AU - Inoue, Shuhei

AU - Kojima, Kouji

AU - Nishiyama, Yoshitaka

N1 - Funding Information: This work was supported, in part, by a Grant-in-Aid for Scientific Research from the Ministry of Education, Culture, Sports, Science, and Technology of Japan ( no. 21570033 to Y.N.) and by a grant from the Asahi Glass Foundation (to Y.N.). The authors thank Prof. Masahiko Ikeuchi (the University of Tokyo) for providing the pTCP2031 vector. They also thank Mr. Tomohisa Niimi (Saitama University) for radioisotope analysis. Copyright: Copyright 2012 Elsevier B.V., All rights reserved.

PY - 2012/3/23

Y1 - 2012/3/23

N2 - 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.

AB - 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.

KW - Elongation factor G

KW - Oxidative stress

KW - Photoinhibition

KW - Photosystem II

KW - Protein synthesis

KW - Repair

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