메뉴 건너뛰기




Volumn 287, Issue 34, 2012, Pages 28697-28704

Elongation factor G is a critical target during oxidative damage to the translation system of Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE RESIDUES; DISULFIDE BONDS; E. COLI; ELONGATION FACTOR; IN-VITRO; INTRAMOLECULAR DISULFIDE BONDS; OXIDATIVE DAMAGE; REDOX STATE; REDUCING POWER; THIOREDOXINS; TRANSLATION SYSTEMS; TRANSLATIONAL ELONGATION; UBIQUITOUS PROTEIN;

EID: 84865260282     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.378067     Document Type: Article
Times cited : (20)

References (31)
  • 1
    • 0023987447 scopus 로고
    • Reversible inhibition of DNA and protein synthesis by cumene hydroperoxide and 4-hydroxynonenal
    • Poot, M., Verkerk, A., Koster, J. F., Esterbauer, H., and Jongkind, J. F. (1988) Reversible inhibition of DNA and protein synthesis by cumene hydroperoxide and 4-hydroxynonenal. Mech. Ageing Dev. 43, 1-9
    • (1988) Mech. Ageing Dev. , vol.43 , pp. 1-9
    • Poot, M.1    Verkerk, A.2    Koster, J.F.3    Esterbauer, H.4    Jongkind, J.F.5
  • 2
    • 0028931814 scopus 로고
    • Effect of oxidizing agents and haemin on the phosphorylation of eukaryotic elongation factor 2 in rabbit reticulocyte lysates
    • Nilsson, A., and Nygård, O. (1995) Effect of oxidizing agents and haemin on the phosphorylation of eukaryotic elongation factor 2 in rabbit reticulocyte lysates. Biochim. Biophys. Acta 1260, 200-206
    • (1995) Biochim. Biophys. Acta , vol.1260 , pp. 200-206
    • Nilsson, A.1    Nygård, O.2
  • 3
    • 0032579371 scopus 로고    scopus 로고
    • Identification of the major oxidatively damaged proteins in Escherichia coli cells exposed to oxidative stress
    • Tamarit, J., Cabiscol, E., and Ros, J. (1998) Identification of the major oxidatively damaged proteins in Escherichia coli cells exposed to oxidative stress. J. Biol. Chem. 273, 3027-3032
    • (1998) J. Biol. Chem. , vol.273 , pp. 3027-3032
    • Tamarit, J.1    Cabiscol, E.2    Ros, J.3
  • 4
    • 0034282468 scopus 로고    scopus 로고
    • Oxidative stress promotes specific protein damage in Saccharomyces cerevisiae
    • Cabiscol, E., Piulats, E., Echave, P., Herrero, E., and Ros, J. (2000) Oxidative stress promotes specific protein damage in Saccharomyces cerevisiae. J. Biol. Chem. 275, 27393-27398
    • (2000) J. Biol. Chem. , vol.275 , pp. 27393-27398
    • Cabiscol, E.1    Piulats, E.2    Echave, P.3    Herrero, E.4    Ros, J.5
  • 5
    • 0033543618 scopus 로고    scopus 로고
    • Oxidative stress defense and deterioration of growth-arrested Escherichia coli cells
    • Dukan, S., and Nyström, T. (1999) Oxidative stress defense and deterioration of growth-arrested Escherichia coli cells. J. Biol. Chem. 274, 26027-26032
    • (1999) J. Biol. Chem. , vol.274 , pp. 26027-26032
    • Dukan, S.1    Nyström, T.2
  • 6
    • 0029841946 scopus 로고    scopus 로고
    • Effect of oxidative stress, produced by cumene hydroperoxide, on the various steps of protein synthesis. Modifications of elongation factor-2
    • Ayala, A., Parrado, J., Bougria, M., and Machado, A. (1996) Effect of oxidative stress, produced by cumene hydroperoxide, on the various steps of protein synthesis. Modifications of elongation factor-2. J. Biol. Chem. 271, 23105-23110
    • (1996) J. Biol. Chem. , vol.271 , pp. 23105-23110
    • Ayala, A.1    Parrado, J.2    Bougria, M.3    Machado, A.4
  • 7
    • 79954467937 scopus 로고    scopus 로고
    • Protein synthesis is the primary target of reactive oxygen species in the photoinhibition of photosystem II
    • Nishiyama, Y., Allakhverdiev, S. I., and Murata, N. (2011) Protein synthesis is the primary target of reactive oxygen species in the photoinhibition of photosystem II. Physiol Plant 142, 35-46
    • (2011) Physiol Plant , vol.142 , pp. 35-46
    • Nishiyama, Y.1    Allakhverdiev, S.I.2    Murata, N.3
  • 8
    • 0035886704 scopus 로고    scopus 로고
    • Oxidative stress inhibits the repair of photodamage to the photosynthetic machinery
    • Nishiyama, Y., Yamamoto, H., Allakhverdiev, S. I., Inaba, M., Yokota, A., and Murata, N. (2001) Oxidative stress inhibits the repair of photodamage to the photosynthetic machinery. EMBO J. 20, 5587-5594
    • (2001) EMBO J. , vol.20 , pp. 5587-5594
    • Nishiyama, Y.1    Yamamoto, H.2    Allakhverdiev, S.I.3    Inaba, M.4    Yokota, A.5    Murata, N.6
  • 9
    • 4444313478 scopus 로고    scopus 로고
    • Singlet oxygen inhibits the repair of photosystem II by suppressing the translation elongation of the D1 protein in Synechocystis sp. PCC 6803
    • Nishiyama, Y., Allakhverdiev, S. I., Yamamoto, H., Hayashi, H., and Murata, N. (2004) Singlet oxygen inhibits the repair of photosystem II by suppressing the translation elongation of the D1 protein in Synechocystis sp. PCC 6803. Biochemistry 43, 11321-11330
    • (2004) Biochemistry , vol.43 , pp. 11321-11330
    • Nishiyama, Y.1    Allakhverdiev, S.I.2    Yamamoto, H.3    Hayashi, H.4    Murata, N.5
  • 10
    • 34547669234 scopus 로고    scopus 로고
    • Oxidation of elongation factor G inhibits the synthesis of the D1 protein of photosystem II
    • Kojima, K., Oshita, M., Nanjo, Y., Kasai, K., Tozawa, Y., Hayashi, H., and Nishiyama, Y. (2007) Oxidation of elongation factor G inhibits the synthesis of the D1 protein of photosystem II. Mol. Microbiol. 65, 936-947
    • (2007) Mol. Microbiol. , vol.65 , pp. 936-947
    • Kojima, K.1    Oshita, M.2    Nanjo, Y.3    Kasai, K.4    Tozawa, Y.5    Hayashi, H.6    Nishiyama, Y.7
  • 11
    • 67650541841 scopus 로고    scopus 로고
    • Regulation of translation by the redox state of elongation factor G in the cyanobacterium Synechocystis sp. PCC 6803
    • Kojima, K., Motohashi, K., Morota, T., Oshita, M., Hisabori, T., Hayashi, H., and Nishiyama, Y. (2009) Regulation of translation by the redox state of elongation factor G in the cyanobacterium Synechocystis sp. PCC 6803. J. Biol. Chem. 284, 18685-18691
    • (2009) J. Biol. Chem. , vol.284 , pp. 18685-18691
    • Kojima, K.1    Motohashi, K.2    Morota, T.3    Oshita, M.4    Hisabori, T.5    Hayashi, H.6    Nishiyama, Y.7
  • 14
    • 71549130134 scopus 로고    scopus 로고
    • Jacquot, J.-P., ed Academic Press, Burlington, VT
    • Hisabori, T., and Nishiyama, Y. (2009) in Advances in Botanical Research (Jacquot, J.-P., ed) Vol. 52, pp. 187-205, Academic Press, Burlington, VT
    • (2009) Advances in Botanical Research , vol.52 , pp. 187-205
    • Hisabori, T.1    Nishiyama, Y.2
  • 16
    • 0037154986 scopus 로고    scopus 로고
    • Ribosome structure and the mechanism of translation
    • Ramakrishnan, V. (2002) Ribosome structure and the mechanism of translation. Cell 108, 557-572
    • (2002) Cell , vol.108 , pp. 557-572
    • Ramakrishnan, V.1
  • 17
    • 70149110001 scopus 로고    scopus 로고
    • Detecting folding intermediates of a protein as it passes through the bacterial translocation channel
    • Kadokura, H., and Beckwith, J. (2009) Detecting folding intermediates of a protein as it passes through the bacterial translocation channel. Cell 138, 1164-1173
    • (2009) Cell , vol.138 , pp. 1164-1173
    • Kadokura, H.1    Beckwith, J.2
  • 18
  • 19
    • 84859432765 scopus 로고    scopus 로고
    • Structural insights into initial and intermediate steps of the ribosome-recycling process
    • Yokoyama, T., Shaikh, T. R., Iwakura, N., Kaji, H., Kaji, A., and Agrawal, R. K. (2012) Structural insights into initial and intermediate steps of the ribosome-recycling process. EMBO J. 31, 1836-1846
    • (2012) EMBO J. , vol.31 , pp. 18361846
    • Yokoyama, T.1    Shaikh, T.R.2    Iwakura, N.3    Kaji, H.4    Kaji, A.5    Agrawal, R.K.6
  • 20
    • 0016220086 scopus 로고
    • The role of guanosine triphosphate in translocation reaction catalyzed by elongation factor G
    • Inoue-Yokosawa, N., Ishikawa, C., and Kaziro, Y. (1974) The role of guanosine triphosphate in translocation reaction catalyzed by elongation factor G. J. Biol. Chem. 249, 4321-4323
    • (1974) J. Biol. Chem. , vol.249 , pp. 4321-4323
    • Inoue-Yokosawa, N.1    Ishikawa, C.2    Kaziro, Y.3
  • 21
    • 0035800829 scopus 로고    scopus 로고
    • Mutations in the G-domain of elongation factorGfrom Thermus thermophilus affect both its interaction with GTP and fusidic acid
    • Martemyanov, K. A., Liljas, A., Yarunin, A. S., and Gudkov, A. T. (2001) Mutations in the G-domain of elongation factorGfrom Thermus thermophilus affect both its interaction with GTP and fusidic acid. J. Biol. Chem. 276, 28774-28778
    • (2001) J. Biol. Chem. , vol.276 , pp. 28774-28778
    • Martemyanov, K.A.1    Liljas, A.2    Yarunin, A.S.3    Gudkov, A.T.4
  • 22
    • 73349133007 scopus 로고    scopus 로고
    • Thioredoxins and glutaredoxins. Unifying elements in redox biology
    • Meyer, Y., Buchanan, B. B., Vignols, F., and Reichheld, J. P. (2009) Thioredoxins and glutaredoxins. Unifying elements in redox biology. Annu. Rev. Genet. 43, 335-367
    • (2009) Annu. Rev. Genet. , vol.43 , pp. 335-367
    • Meyer, Y.1    Buchanan, B.B.2    Vignols, F.3    Reichheld, J.P.4
  • 23
    • 1642363933 scopus 로고    scopus 로고
    • Proteomic analysis of thioredoxin-targeted proteins in Escherichia coli
    • Kumar, J. K., Tabor, S., and Richardson, C. C. (2004) Proteomic analysis of thioredoxin-targeted proteins in Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 101, 3759-3764
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 3759-3764
    • Kumar, J.K.1    Tabor, S.2    Richardson, C.C.3
  • 24
    • 34447518686 scopus 로고    scopus 로고
    • The system biology of thiol redox system in Escherichia coli and yeast. Differential functions in oxidative stress, iron metabolism, and DNA synthesis
    • Toledano, M. B., Kumar, C., Le Moan, N., Spector, D., and Tacnet, F. (2007) The system biology of thiol redox system in Escherichia coli and yeast. Differential functions in oxidative stress, iron metabolism, and DNA synthesis. FEBS Lett. 581, 3598-3607
    • (2007) FEBS Lett. , vol.581 , pp. 3598-3607
    • Toledano, M.B.1    Kumar, C.2    Le Moan, N.3    Spector, D.4    Tacnet, F.5
  • 26
    • 0027739665 scopus 로고
    • Mutations that allow disulfide bond formation in the cytoplasm of Escherichia coli
    • Derman, A. I., Prinz, W. A., Belin, D., and Beckwith, J. (1993) Mutations that allow disulfide bond formation in the cytoplasm of Escherichia coli. Science 262, 1744-1747
    • (1993) Science , vol.262 , pp. 1744-1747
    • Derman, A.I.1    Prinz, W.A.2    Belin, D.3    Beckwith, J.4
  • 27
    • 84858706742 scopus 로고    scopus 로고
    • A change in the sensitivity of elongation factor G to oxidation protects photosystem II from photoinhibition in Synechocystis sp. PCC 6803
    • Ejima, K., Kawaharada, T., Inoue, S., Kojima, K., and Nishiyama, Y. (2012) A change in the sensitivity of elongation factor G to oxidation protects photosystem II from photoinhibition in Synechocystis sp. PCC 6803. FEBS Lett. 586, 778-783
    • (2012) FEBS Lett. , vol.586 , pp. 778-783
    • Ejima, K.1    Kawaharada, T.2    Inoue, S.3    Kojima, K.4    Nishiyama, Y.5
  • 28
    • 0033572660 scopus 로고    scopus 로고
    • Targeted mRNA degradation by double-stranded RNA in vitro
    • Tuschl, T., Zamore, P. D., Lehmann, R., Bartel, D. P., and Sharp, P. A. (1999) Targeted mRNA degradation by double-stranded RNA in vitro. Genes Dev. 13, 3191-3197
    • (1999) Genes Dev. , vol.13 , pp. 3191-3197
    • Tuschl, T.1    Zamore, P.D.2    Lehmann, R.3    Bartel, D.P.4    Sharp, P.A.5
  • 29
    • 0034681174 scopus 로고    scopus 로고
    • A highly efficient and robust cell-free protein synthesis system prepared from wheat embryos. Plants apparently contain a suicide system directed at ribosomes
    • Madin, K., Sawasaki, T., Ogasawara, T., and Endo, Y. (2000) A highly efficient and robust cell-free protein synthesis system prepared from wheat embryos. Plants apparently contain a suicide system directed at ribosomes. Proc. Natl. Acad. Sci. U.S.A. 97, 559-564
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 559-564
    • Madin, K.1    Sawasaki, T.2    Ogasawara, T.3    Endo, Y.4
  • 30
    • 0029971659 scopus 로고    scopus 로고
    • Cis-acting elements and trans-acting factors for accurate translation of chloroplast psbA mRNAs. Development of an in vitro translation system from tobacco chloroplasts
    • Hirose, T., and Sugiura, M. (1996) Cis-acting elements and trans-acting factors for accurate translation of chloroplast psbA mRNAs. Development of an in vitro translation system from tobacco chloroplasts. EMBO J. 15, 1687-1695
    • (1996) EMBO J. , vol.15 , pp. 1687-1695
    • Hirose, T.1    Sugiura, M.2
  • 31
    • 70449720539 scopus 로고    scopus 로고
    • Expression of human Cu,Zn-superoxide dismutase in an insect cell-free system and its structural analysis by MALDI-TOF MS
    • Ezure, T., Suzuki, T., Ando, E., Nishimura, O., and Tsunasawa, S. (2009) Expression of human Cu,Zn-superoxide dismutase in an insect cell-free system and its structural analysis by MALDI-TOF MS. J Biotechnol 144, 287-292
    • (2009) J Biotechnol , vol.144 , pp. 287-292
    • Ezure, T.1    Suzuki, T.2    Ando, E.3    Nishimura, O.4    Tsunasawa, S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.