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Volumn 16, Issue 13, 1997, Pages 4134-4141

Fast recycling of Escherichia coli ribosomes requires both ribosome recycling factor (RRF) and release factor RF3

Author keywords

In vitro translation; Release factors; Ribosome recycling

Indexed keywords

AMINO ACID TRANSFER RNA LIGASE; ELONGATION FACTOR G; MESSENGER RNA; POLYPEPTIDE; PROTEIN; RELEASE FACTOR 3; RIBOSOME RECYCLING FACTOR; UNCLASSIFIED DRUG;

EID: 0030928327     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/16.13.4134     Document Type: Article
Times cited : (114)

References (34)
  • 1
    • 0028357882 scopus 로고
    • The concentration of polypeptide chain release factors 1 and 2 at different growth rates of Escherichia coli
    • Adamski, F.M., McCaughan, K.K., Jørgensen, F., Kurland, C.G. and Tate, W.P. (1994) The concentration of polypeptide chain release factors 1 and 2 at different growth rates of Escherichia coli. J. Mol. Biol., 238, 302-308.
    • (1994) J. Mol. Biol. , vol.238 , pp. 302-308
    • Adamski, F.M.1    McCaughan, K.K.2    Jørgensen, F.3    Kurland, C.G.4    Tate, W.P.5
  • 2
    • 0025341309 scopus 로고
    • Scanning model for translational reinitiation in eubacteria
    • Adhin, M.R. and van Duin, J. (1990) Scanning model for translational reinitiation in eubacteria. J. Mol. Biol., 213, 811-818.
    • (1990) J. Mol. Biol. , vol.213 , pp. 811-818
    • Adhin, M.R.1    Van Duin, J.2
  • 3
    • 0021929046 scopus 로고
    • Manipulation of intracellular magnesium content in polymyxin B nonapeptide-sensitized Escherichia coli by ionophore A23187
    • Alatossava, T., Jutte, H., Kuhn, A. and Kellenberger, E. (1985) Manipulation of intracellular magnesium content in polymyxin B nonapeptide-sensitized Escherichia coli by ionophore A23187. J. Bacteriol., 162, 413-419.
    • (1985) J. Bacteriol. , vol.162 , pp. 413-419
    • Alatossava, T.1    Jutte, H.2    Kuhn, A.3    Kellenberger, E.4
  • 4
    • 0000640710 scopus 로고    scopus 로고
    • Modulation of chemical composition and other parameters of the cell by growth rate
    • Neidhart,F.C. (ed.), ASM Press, Washington DC
    • Bremer, H. and Dennis, P.P. (1996) Modulation of chemical composition and other parameters of the cell by growth rate. In Neidhart,F.C. (ed.), Escherichia coli and Salmonella. 2nd edn. ASM Press, Washington DC, vol. 2, pp. 1553-1569.
    • (1996) Escherichia Coli and Salmonella. 2nd Edn. , vol.2 , pp. 1553-1569
    • Bremer, H.1    Dennis, P.P.2
  • 5
    • 0027853904 scopus 로고
    • Translational regulation of the Escherichia coli threonyl-tRNA synthetase gene: Structural and functional importance of the thrS operator domains
    • Brunel, C., Romby, P., Moine, H., Caillet, J., Grunberg-Manago, M., Springer, M., Ehresmann, B. and Ehresmann, C. (1993) Translational regulation of the Escherichia coli threonyl-tRNA synthetase gene: structural and functional importance of the thrS operator domains. Biochimie, 75, 1167-1179.
    • (1993) Biochimie , vol.75 , pp. 1167-1179
    • Brunel, C.1    Romby, P.2    Moine, H.3    Caillet, J.4    Grunberg-Manago, M.5    Springer, M.6    Ehresmann, B.7    Ehresmann, C.8
  • 6
    • 0347992111 scopus 로고
    • Selection of the mRNA translation initiation region by Escherichia coli ribosomes
    • Calogero, R.A., Pon, C.L., Canonaco, M.A. and Gualerzi, C.O. (1988) Selection of the mRNA translation initiation region by Escherichia coli ribosomes. Proc. Natl Acad. Sci. USA, 85, 6427-6431.
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 6427-6431
    • Calogero, R.A.1    Pon, C.L.2    Canonaco, M.A.3    Gualerzi, C.O.4
  • 7
    • 0023643112 scopus 로고
    • Translational frameshifting: Where will it stop?
    • Craigen, W.J. and Caskey, C.T. (1987) Translational frameshifting: where will it stop? Cell, 50, 1-2.
    • (1987) Cell , vol.50 , pp. 1-2
    • Craigen, W.J.1    Caskey, C.T.2
  • 8
    • 0342423297 scopus 로고
    • Studies of the binding of turnip yellow mosaic virus RNA to Escherichia coli ribosomes
    • Dahlberg, J.E. and Haselkorn, R. (1967) Studies of the binding of turnip yellow mosaic virus RNA to Escherichia coli ribosomes. J. Mol. Biol., 24, 83-104.
    • (1967) J. Mol. Biol. , vol.24 , pp. 83-104
    • Dahlberg, J.E.1    Haselkorn, R.2
  • 9
    • 0000332840 scopus 로고
    • Design and use of a fast and accurate in vitro translation system
    • Spedding,G. (ed.), IRL Press at Oxford University Press
    • Ehrenberg, M., Bilgin, N. and Kurland, C.G. (1990) Design and use of a fast and accurate in vitro translation system. In Spedding,G. (ed.), Ribosomes and Protein Synthesis - A Practical Approach. IRL Press at Oxford University Press, pp. 101-129.
    • (1990) Ribosomes and Protein Synthesis - A Practical Approach , pp. 101-129
    • Ehrenberg, M.1    Bilgin, N.2    Kurland, C.G.3
  • 10
    • 0030949960 scopus 로고    scopus 로고
    • Release factor RF3 in E.coli accelerates the dissociation of release factors RF1 and RF2 from the ribosome in a GTP dependent manner
    • Freistroffer, D., Pavlov, M., MacDougall, J., Buckingham, R.H. and Ehrenberg, M. (1997) Release factor RF3 in E.coli accelerates the dissociation of release factors RF1 and RF2 from the ribosome in a GTP dependent manner. EMBO J., 16, 4126-4133.
    • (1997) EMBO J. , vol.16 , pp. 4126-4133
    • Freistroffer, D.1    Pavlov, M.2    MacDougall, J.3    Buckingham, R.H.4    Ehrenberg, M.5
  • 11
    • 0028581973 scopus 로고
    • A highly conserved eukaryotic protein family possessing properties of polypeptide chain release factor
    • Frolova, L. et al. (1994) A highly conserved eukaryotic protein family possessing properties of polypeptide chain release factor. Nature, 372, 701-703.
    • (1994) Nature , vol.372 , pp. 701-703
    • Frolova, L.1
  • 12
    • 0014854959 scopus 로고
    • Peptide chain termination: Effect of protein S on ribosomal binding of release factors
    • Goldstein, J.L. and Caskey, C.T. (1970) Peptide chain termination: effect of protein S on ribosomal binding of release factors. Proc. Natl Acad. Sci. USA, 67, 537-543.
    • (1970) Proc. Natl Acad. Sci. USA , vol.67 , pp. 537-543
    • Goldstein, J.L.1    Caskey, C.T.2
  • 13
    • 0014734478 scopus 로고
    • Peptide chain termination, VI: Purification and site of action of S
    • Goldstein, J., Milman, G., Scolnick, E. and Caskey, T. (1970) Peptide chain termination, VI: purification and site of action of S. Proc. Natl Acad. Sci. USA, 65, 430-437.
    • (1970) Proc. Natl Acad. Sci. USA , vol.65 , pp. 430-437
    • Goldstein, J.1    Milman, G.2    Scolnick, E.3    Caskey, T.4
  • 14
    • 0028012044 scopus 로고
    • Effect of sequence context at stop codons on efficiency of reinitiation in GCN4 translational control
    • Grant, C.M. and Hinnebusch, A.G. (1994) Effect of sequence context at stop codons on efficiency of reinitiation in GCN4 translational control. Mol. Cell. Biol., 14, 606-618.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 606-618
    • Grant, C.M.1    Hinnebusch, A.G.2
  • 17
    • 0015887427 scopus 로고
    • Role of elongation factor G and a protein factor in the release of ribosomes from messenger ribonucleic acid
    • Hirashima, A. and Kaji, A. (1973) Role of elongation factor G and a protein factor in the release of ribosomes from messenger ribonucleic acid. J. Biol. Chem., 248, 7580-7587.
    • (1973) J. Biol. Chem. , vol.248 , pp. 7580-7587
    • Hirashima, A.1    Kaji, A.2
  • 18
    • 0028314657 scopus 로고
    • Ribosome recycling factor (ribosome releasing factor) is essential for bacterial growth
    • Janosi, L., Shimizu, I. and Kaji, A. (1994) Ribosome recycling factor (ribosome releasing factor) is essential for bacterial growth. Proc. Natl Acad. Sci. USA, 91, 4249-4253.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 4249-4253
    • Janosi, L.1    Shimizu, I.2    Kaji, A.3
  • 19
    • 0029950071 scopus 로고    scopus 로고
    • Ribosome recycling by ribosome recycling factor (RRF) - An important but overlooked step of protein synthesis
    • Janosi, L., Hara, H., Zhang, S. and Kaji, A. (1996) Ribosome recycling by ribosome recycling factor (RRF) - an important but overlooked step of protein synthesis. Adv. Biophys., 32, 121-201.
    • (1996) Adv. Biophys. , vol.32 , pp. 121-201
    • Janosi, L.1    Hara, H.2    Zhang, S.3    Kaji, A.4
  • 20
    • 0019119293 scopus 로고
    • Rapid purification of highly active ribosomes from Escherichia coli
    • Jelenc, P.C. (1980) Rapid purification of highly active ribosomes from Escherichia coli. Anal. Biochem., 105, 369-374.
    • (1980) Anal. Biochem. , vol.105 , pp. 369-374
    • Jelenc, P.C.1
  • 21
    • 0018498843 scopus 로고
    • Nucleotide triphosphate regeneration decreases the frequency of translation errors
    • Jelenc, P.C. and Kurland, C.G. (1979) Nucleotide triphosphate regeneration decreases the frequency of translation errors. Proc. Natl Acad. Sci. USA, 76, 3174-3178.
    • (1979) Proc. Natl Acad. Sci. USA , vol.76 , pp. 3174-3178
    • Jelenc, P.C.1    Kurland, C.G.2
  • 22
    • 0029986817 scopus 로고    scopus 로고
    • Dissociation rates of peptidyl-tRNA from the P-site of E.coli ribosomes
    • Karimi, R. and Ehrenberg, M. (1996) Dissociation rates of peptidyl-tRNA from the P-site of E.coli ribosomes. EMBO J., 15, 1149-1154
    • (1996) EMBO J. , vol.15 , pp. 1149-1154
    • Karimi, R.1    Ehrenberg, M.2
  • 23
    • 0015239117 scopus 로고
    • Polypetide chain termination. Purification of the release factors, R1 and R2, from Escherichia coli
    • Klein, H. and Capecchi, M.R. (1971) Polypetide chain termination. Purification of the release factors, R1 and R2, from Escherichia coli. J. Biol. Chem., 246, 1055-1061.
    • (1971) J. Biol. Chem. , vol.246 , pp. 1055-1061
    • Klein, H.1    Capecchi, M.R.2
  • 24
    • 0029912348 scopus 로고    scopus 로고
    • Suppression of temperature-sensitive defects of polypeptide release factors RF-1 and RF-2 by mutations or by an excess of RF-3 in Escherichia coli
    • Matsumura, K., Ito, K., Kawazu, Y., Mikuni, O. and Nakamura, Y. (1996) Suppression of temperature-sensitive defects of polypeptide release factors RF-1 and RF-2 by mutations or by an excess of RF-3 in Escherichia coli. J. Mol. Biol., 258, 588-599.
    • (1996) J. Mol. Biol. , vol.258 , pp. 588-599
    • Matsumura, K.1    Ito, K.2    Kawazu, Y.3    Mikuni, O.4    Nakamura, Y.5
  • 26
    • 0014516109 scopus 로고
    • Peptide chain termination: III. Stimulation of in vitro termination
    • Milman, G., Goldstein, J., Scolnick, E. and Caskey, T. (1969) Peptide chain termination: III. Stimulation of in vitro termination. Proc. Natl Acad. Sci. USA, 63, 183-190.
    • (1969) Proc. Natl Acad. Sci. USA , vol.63 , pp. 183-190
    • Milman, G.1    Goldstein, J.2    Scolnick, E.3    Caskey, T.4
  • 27
    • 0030592511 scopus 로고    scopus 로고
    • Emerging understanding of translation termination
    • Nakamura, Y., Ito, K. and Isaksson, L.A. (1996) Emerging understanding of translation termination. Cell, 87, 147-150.
    • (1996) Cell , vol.87 , pp. 147-150
    • Nakamura, Y.1    Ito, K.2    Isaksson, L.A.3
  • 28
    • 0029873397 scopus 로고    scopus 로고
    • Rate of translation of natural mRNAs in an optimised in vitro translation system
    • Pavlov, M.Yu. and Ehrenberg, M. (1996) Rate of translation of natural mRNAs in an optimised in vitro translation system. Arch. Biochem. Biophys., 328, 9-16.
    • (1996) Arch. Biochem. Biophys. , vol.328 , pp. 9-16
    • Pavlov, M.Yu.1    Ehrenberg, M.2
  • 29
    • 0343927238 scopus 로고
    • Reinitiation of translation from the triplet next to the amber termination codon in the absence of ribosome-releasing factor
    • Ryoji, M., Berland, R. and Kaji, A. (1981) Reinitiation of translation from the triplet next to the amber termination codon in the absence of ribosome-releasing factor. Proc. Natl Acad. Sci. USA, 78, 5973.
    • (1981) Proc. Natl Acad. Sci. USA , vol.78 , pp. 5973
    • Ryoji, M.1    Berland, R.2    Kaji, A.3
  • 31
    • 0026608933 scopus 로고
    • Translational termination - Stop for protein synthesis or pause for regulation of gene expression
    • Tate, W.P. and Brown, C.M. (1992) Translational termination - stop for protein synthesis or pause for regulation of gene expression. Biochemistry, 31, 2443-2450.
    • (1992) Biochemistry , vol.31 , pp. 2443-2450
    • Tate, W.P.1    Brown, C.M.2
  • 32
    • 0002998552 scopus 로고
    • Termination of protein synthesis
    • Spedding, G. (ed.), IRL Press at Oxford University Press
    • Tate, W.P. and Caskey, C.T. (1990) Termination of protein synthesis. In Spedding, G. (ed.), Ribosomes and Protein Synthesis - A Practical Approach, IRL Press at Oxford University Press, pp. 81-100.
    • (1990) Ribosomes and Protein Synthesis - A Practical Approach , pp. 81-100
    • Tate, W.P.1    Caskey, C.T.2
  • 33
    • 0029773416 scopus 로고    scopus 로고
    • Three, four or more: The translational stop signal at length
    • Tate, W.P. and Mannering, S.A. (1996) Three, four or more: the translational stop signal at length. Mol. Microbiol., 21, 213-219.
    • (1996) Mol. Microbiol. , vol.21 , pp. 213-219
    • Tate, W.P.1    Mannering, S.A.2
  • 34
    • 0029145925 scopus 로고
    • Termination of translation in eukaryotes is governed by two interacting polypeptide chain release factors, eRF1 and eRF3
    • Zhouravleva, G., Frolova, L., Le Goff, X., Le Guellec, R., Inge-Vechtomov, S., Kisselev, L. and Philippe, M. (1995) Termination of translation in eukaryotes is governed by two interacting polypeptide chain release factors, eRF1 and eRF3. EMBO J., 14, 4065-4072.
    • (1995) EMBO J. , vol.14 , pp. 4065-4072
    • Zhouravleva, G.1    Frolova, L.2    Le Goff, X.3    Le Guellec, R.4    Inge-Vechtomov, S.5    Kisselev, L.6    Philippe, M.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.