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Volumn 4, Issue 8, 1998, Pages 973-983

Release factor RF-3 GTPase activity acts in disassembly of the ribosome termination complex

Author keywords

GTPase; RF1; RF2; RRF; Translation

Indexed keywords

GUANOSINE TRIPHOSPHATASE; TRANSLATION TERMINATION FACTOR;

EID: 0031825179     PISSN: 13558382     EISSN: None     Source Type: Journal    
DOI: 10.1017/S1355838298971576     Document Type: Article
Times cited : (45)

References (58)
  • 1
    • 0028357882 scopus 로고
    • The concentration of polypeptide chain release factors 1 and 2 at different growth rates of Escherichia coli
    • Adamski FM, McCaughan KK, Jorgensen F, Kurland CG, Tate WP. 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    Jorgensen, F.3    Kurland, C.G.4    Tate, W.P.5
  • 2
    • 0018785330 scopus 로고
    • Cation-induced regulatory mechanism of GTPase activity dependent on polypeptide initiation factor 2
    • Beaudry P, Sander G, Grunberg-Manago M, Douzou P. 1979. Cation-induced regulatory mechanism of GTPase activity dependent on polypeptide initiation factor 2. Biochemistry 18:202-207.
    • (1979) Biochemistry , vol.18 , pp. 202-207
    • Beaudry, P.1    Sander, G.2    Grunberg-Manago, M.3    Douzou, P.4
  • 3
    • 0015975563 scopus 로고
    • The requirement for ribosomal proteins L7/L12 in peptide chain termination
    • Brot N, Tate WP, Caskey CT, Weissbach H. 1974. The requirement for ribosomal proteins L7/L12 in peptide chain termination. Proc Natl Acad of Sci USA 71:89-92.
    • (1974) Proc Natl Acad of Sci USA , vol.71 , pp. 89-92
    • Brot, N.1    Tate, W.P.2    Caskey, C.T.3    Weissbach, H.4
  • 5
    • 0014126461 scopus 로고
    • Polypeptide chain termination in vitro: Isolation of a release factor
    • Capecchi MR. 1967. Polypeptide chain termination in vitro: Isolation of a release factor. Proc Natl Acad Sci USA 58:1144-1151.
    • (1967) Proc Natl Acad Sci USA , vol.58 , pp. 1144-1151
    • Capecchi, M.R.1
  • 6
    • 0014631155 scopus 로고
    • Characterization of three proteins involved in polypeptide chain termination
    • Capecchi MR, Klein HA. 1969. Characterization of three proteins involved in polypeptide chain termination. Cold Spring Harbor Symp Quant Biol 34:469-477.
    • (1969) Cold Spring Harbor Symp Quant Biol , vol.34 , pp. 469-477
    • Capecchi, M.R.1    Klein, H.A.2
  • 7
    • 0011976947 scopus 로고
    • Peptide chain termination
    • Weissbach H, Pestka S, eds. New York: Academic Press
    • Caskey CT. 1977. Peptide chain termination. In: Weissbach H, Pestka S, eds. Molecular mechanisms of protein biosynthesis. New York: Academic Press, pp 443-465.
    • (1977) Molecular Mechanisms of Protein Biosynthesis , pp. 443-465
    • Caskey, C.T.1
  • 10
    • 0014402968 scopus 로고
    • Sequential translation of trinucleotide codons for initiation and termination of protein synthesis
    • Caskey CT, Tompkins R, Scolnick E, Caryk T, Nierenberg M. 1968. Sequential translation of trinucleotide codons for initiation and termination of protein synthesis. Science 162:135-138.
    • (1968) Science , vol.162 , pp. 135-138
    • Caskey, C.T.1    Tompkins, R.2    Scolnick, E.3    Caryk, T.4    Nierenberg, M.5
  • 11
    • 78651145301 scopus 로고
    • Characterization of a ribosome-linked guanosine triphosphatase in Escherichia coli extracts
    • Conway TW, Lipmann F. 1964. Characterization of a ribosome-linked guanosine triphosphatase in Escherichia coli extracts. Proc Natl Acad Sci USA 52:1462-1469.
    • (1964) Proc Natl Acad Sci USA , vol.52 , pp. 1462-1469
    • Conway, T.W.1    Lipmann, F.2
  • 12
    • 0001374853 scopus 로고
    • Mass spectrometric techniques in nucleic acid research
    • Crain PF. 1990. Mass spectrometric techniques in nucleic acid research. Mass Spectrom Rev 9:505-554.
    • (1990) Mass Spectrom Rev , vol.9 , pp. 505-554
    • Crain, P.F.1
  • 14
    • 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 DV, Pavlov MY, McDougall J, Buckingham RH, 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 16:4126-4133.
    • (1997) EMBO , vol.16 , pp. 4126-4133
    • Freistroffer, D.V.1    Pavlov, M.Y.2    McDougall, J.3    Buckingham, R.H.4    Ehrenberg, M.5
  • 16
    • 19244364778 scopus 로고    scopus 로고
    • Eukaryotic polypeptide chain release factor eRF3 is an eRF1- and ribosome-dependent guanosine triphosphatase
    • Frolova L, LeGoff X, Zhouravleva G, Davydova E, Philippe M, Kisselev L. 1996. Eukaryotic polypeptide chain release factor eRF3 is an eRF1- and ribosome-dependent guanosine triphosphatase. RNA 2:334-341.
    • (1996) RNA , vol.2 , pp. 334-341
    • Frolova, L.1    LeGoff, X.2    Zhouravleva, G.3    Davydova, E.4    Philippe, M.5    Kisselev, L.6
  • 17
    • 0345309157 scopus 로고
    • Polypeptide chain termination in cell-free extracts of E. coli
    • Ganoza MC. 1966. Polypeptide chain termination in cell-free extracts of E. coli. Cold Spring Harbor Symp Quant Biol 37:263-268.
    • (1966) Cold Spring Harbor Symp Quant Biol , vol.37 , pp. 263-268
    • Ganoza, M.C.1
  • 18
    • 0013872225 scopus 로고
    • Studies on the mechanism of polypeptide chain termination in cell-free extracts of E. coli
    • Ganoza MC, Nakamoto T. 1966. Studies on the mechanism of polypeptide chain termination in cell-free extracts of E. coli Proc Natl Acad Sci USA 55:162-169.
    • (1966) Proc Natl Acad Sci USA , vol.55 , pp. 162-169
    • Ganoza, M.C.1    Nakamoto, T.2
  • 20
    • 0014854959 scopus 로고
    • Peptide chain termination: Effect of protein S on ribosomal binding of release factors
    • Goldstein JL, Caskey CT. 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
  • 21
  • 23
    • 0028932607 scopus 로고
    • Function of polypeptide chain release factor RF-3 in Escherichia coli. RF-3 action in termination is predominantly at UGA-containing stop signals
    • Grentzmann G, Brechemier-Baey D, Heurgue-Hamard V, Buckingham RH. 1995. Function of polypeptide chain release factor RF-3 in Escherichia coli. RF-3 action in termination is predominantly at UGA-containing stop signals. J Biol Chem 260:10595-10600.
    • (1995) J Biol Chem , vol.260 , pp. 10595-10600
    • Grentzmann, G.1    Brechemier-Baey, D.2    Heurgue-Hamard, V.3    Buckingham, R.H.4
  • 25
    • 0030995429 scopus 로고    scopus 로고
    • Ribosomal binding site of release factors RF1 and RF2. a new translational termination assay in vitro
    • Grentzmann G, Kelly PJ. 1997. Ribosomal binding site of release factors RF1 and RF2. A new translational termination assay in vitro. J Biol Chem 272:12300-12304.
    • (1997) J Biol Chem , vol.272 , pp. 12300-12304
    • Grentzmann, G.1    Kelly, P.J.2
  • 26
    • 0038351296 scopus 로고    scopus 로고
    • Ribosome release factor RF4 and termination factor RF3 are involved in dissociation of peptidyl-tRNA from the ribosome
    • Heurgué-Hamard V, Mora L, MacDougall J, Leboeuf C, Grentzmann G, Ehrenberg M, Buckingham RH. 1998. Ribosome release factor RF4 and termination factor RF3 are involved in dissociation of peptidyl-tRNA from the ribosome. EMBO J 17:808-816.
    • (1998) EMBO J , vol.17 , pp. 808-816
    • Heurgué-Hamard, V.1    Mora, L.2    MacDougall, J.3    Leboeuf, C.4    Grentzmann, G.5    Ehrenberg, M.6    Buckingham, R.H.7
  • 27
    • 0015522129 scopus 로고
    • Purification and properties of ribosome-releasing factor
    • Hirashima A, Kaji A. 1972. Purification and properties of ribosome-releasing factor. Biochemistry 11:4037-4044.
    • (1972) Biochemistry , vol.11 , pp. 4037-4044
    • Hirashima, A.1    Kaji, A.2
  • 28
    • 0024326882 scopus 로고
    • Molecular cloning and expression of ribosome releasing factor
    • Ichikawa S, Kaji A. 1989. Molecular cloning and expression of ribosome releasing factor. J Biol Chem 264:20054-20059.
    • (1989) J Biol Chem , vol.264 , pp. 20054-20059
    • Ichikawa, S.1    Kaji, A.2
  • 29
    • 0029950071 scopus 로고    scopus 로고
    • Ribosome recycling by ribosome recycling factor (RRF) - An important but overlooked step of protein biosynthesis
    • Janosi L, Hara H, Zhang S, Kaji A. 1996. Ribosome recycling by ribosome recycling factor (RRF) - An important but overlooked step of protein biosynthesis. 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
  • 31
    • 0028314657 scopus 로고
    • Ribosome recycling factor (ribosome releasing factor) is essential for bacterial growth
    • Janosi L, Shimizu I, 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
  • 32
    • 0015411506 scopus 로고
    • Studies on polypeptide elongation factor from E. coli. I. Crystalline factor G
    • Kaziro Y, Inoue-Yokosawa N, Kawakita M. 1972. Studies on polypeptide elongation factor from E. coli. I. Crystalline factor G. J Biochem 72:853-863.
    • (1972) J Biochem , vol.72 , pp. 853-863
    • Kaziro, Y.1    Inoue-Yokosawa, N.2    Kawakita, M.3
  • 34
    • 0344229599 scopus 로고    scopus 로고
    • Messenger RNA translation in prokaryotes: GTPase centers associated with translational factors
    • Laalami S, Grentzmann G, Bremaud L, Cenatiempo Y. 1996. Messenger RNA translation in prokaryotes: GTPase centers associated with translational factors. Biochimie 78:577-589.
    • (1996) Biochimie , vol.78 , pp. 577-589
    • Laalami, S.1    Grentzmann, G.2    Bremaud, L.3    Cenatiempo, Y.4
  • 35
    • 0028898603 scopus 로고
    • Characterization of oligonucleotides and nucleic acids by mass spectrometry
    • Limbach PA, Crain PF, McCloskey JA. 1995. Characterization of oligonucleotides and nucleic acids by mass spectrometry. Curr Opin Biotechnol 6:96-102.
    • (1995) Curr Opin Biotechnol , vol.6 , pp. 96-102
    • Limbach, P.A.1    Crain, P.F.2    McCloskey, J.A.3
  • 36
    • 0021766026 scopus 로고
    • The ribosomal binding domain for the bacterial release factors RF-1, RF-2 and RF-3
    • McCaughan KK, Ward CD, Trotman CNA, Tate WP. 1984. The ribosomal binding domain for the bacterial release factors RF-1, RF-2 and RF-3. FEBS Lett 175:90-94.
    • (1984) FEBS Lett , vol.175 , pp. 90-94
    • McCaughan, K.K.1    Ward, C.D.2    Trotman, C.N.A.3    Tate, W.P.4
  • 37
    • 0018340811 scopus 로고
    • Accumulation of peptidyl tRNA is lethal to Escherichia coli
    • Menninger JR. 1979. Accumulation of peptidyl tRNA is lethal to Escherichia coli. J Bacteriol 137:694-696.
    • (1979) J Bacteriol , vol.137 , pp. 694-696
    • Menninger, J.R.1
  • 40
    • 0030592511 scopus 로고    scopus 로고
    • Emerging understanding of translation termination
    • Nakamura Y, Ito K, Isaksson LA. 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
  • 41
    • 0021155247 scopus 로고
    • Regulation of the synthesis of ribosomes and ribosomal components
    • Nomura M, Gourse R, Baughman G. 1984. Regulation of the synthesis of ribosomes and ribosomal components. Annu Rev Biochem 53:75-117.
    • (1984) Annu Rev Biochem , vol.53 , pp. 75-117
    • Nomura, M.1    Gourse, R.2    Baughman, G.3
  • 42
    • 0016717247 scopus 로고
    • Requirement for ribosome-releasing factor for the release of ribosomes at the termination codon
    • Ogawa K, Kaji A. 1975. Requirement for ribosome-releasing factor for the release of ribosomes at the termination codon. Eur J Biochem 58:411-419.
    • (1975) Eur J Biochem , vol.58 , pp. 411-419
    • Ogawa, K.1    Kaji, A.2
  • 43
    • 0019253694 scopus 로고
    • Translational coupling during expression of the tryptophane operon of Escherichia coli
    • Oppenheim DS, Yanofsky C. 1980. Translational coupling during expression of the tryptophane operon of Escherichia coli. Genetics 95:785-795.
    • (1980) Genetics , vol.95 , pp. 785-795
    • Oppenheim, D.S.1    Yanofsky, C.2
  • 44
    • 0030928327 scopus 로고    scopus 로고
    • Fast recycling of Escherichia coli ribosomes requires both ribosome recycling factor (RRF) and release factor RF3
    • Pavlov MY, Freistroffer DV, McDougall J, Buckingham RH, Ehrenberg M. 1997. Fast recycling of Escherichia coli ribosomes requires both ribosome recycling factor (RRF) and release factor RF3. EMBO 16:4134-4141.
    • (1997) EMBO , vol.16 , pp. 4134-4141
    • Pavlov, M.Y.1    Freistroffer, D.V.2    McDougall, J.3    Buckingham, R.H.4    Ehrenberg, M.5
  • 45
    • 0031965576 scopus 로고    scopus 로고
    • Escherichia coli release factor 3: Resolving the paradox of a typical G protein structure and atypical function with guanine nucleotides
    • Pel HJ, Moffat JG, Ito K, Nakamura Y, Tate WP. 1998. Escherichia coli release factor 3: Resolving the paradox of a typical G protein structure and atypical function with guanine nucleotides. RNA 4:47-54.
    • (1998) RNA , vol.4 , pp. 47-54
    • Pel, H.J.1    Moffat, J.G.2    Ito, K.3    Nakamura, Y.4    Tate, W.P.5
  • 46
    • 0018952629 scopus 로고
    • Adenosine 5′-triphosphate leakage does not cause abortive infection of bacteriophage T7 in male Escherichia coli
    • Remes B, Elseviers D. 1980. Adenosine 5′-triphosphate leakage does not cause abortive infection of bacteriophage T7 in male Escherichia coli. J Bacteriol 143:1054-1056.
    • (1980) J Bacteriol , vol.143 , pp. 1054-1056
    • Remes, B.1    Elseviers, D.2
  • 50
    • 0000273963 scopus 로고
    • Negative ion formation in electrospray mass spectrometry
    • Straub RF, Voyksner RD. 1993. Negative ion formation in electrospray mass spectrometry. J Am Soc Mass Spectrom 4:578-587.
    • (1993) J Am Soc Mass Spectrom , vol.4 , pp. 578-587
    • Straub, R.F.1    Voyksner, R.D.2
  • 51
    • 0026608933 scopus 로고
    • Translational termination: "Stop" for protein synthesis or "pause" for regulation of gene expression
    • Tate WP, Brown CM. 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
  • 53
    • 0021287182 scopus 로고
    • The NH2-terminal domain of Escherichia coli ribosomal protein L11. Its three-dimensional location and its role in the binding of release factors 1 and 2
    • Tate WP, Dognin MJ, Noah M, Stöffler-Meilicke M, Stöffler G. 1984. The NH2-terminal domain of Escherichia coli ribosomal protein L11. Its three-dimensional location and its role in the binding of release factors 1 and 2. J Biol Chem 259:7317-7324.
    • (1984) J Biol Chem , vol.259 , pp. 7317-7324
    • Tate, W.P.1    Dognin, M.J.2    Noah, M.3    Stöffler-Meilicke, M.4    Stöffler, G.5
  • 54
    • 0022981651 scopus 로고
    • The ribosomal binding domain of the Escherichia coli release factors. Modification of tyrosine in the N-terminal domain of ribosomal protein L11 affects release factors 1 and 2 differentially
    • Tate WP, McCaughan KK, Ward CD, Sumpter VG, Trotman CNA, Stöffler-Meilicke M, Maly P, Brimacombe R. 1986. The ribosomal binding domain of the Escherichia coli release factors. Modification of tyrosine in the N-terminal domain of ribosomal protein L11 affects release factors 1 and 2 differentially. J Biol Chem 261:2289-2293.
    • (1986) J Biol Chem , vol.261 , pp. 2289-2293
    • Tate, W.P.1    McCaughan, K.K.2    Ward, C.D.3    Sumpter, V.G.4    Trotman, C.N.A.5    Stöffler-Meilicke, M.6    Maly, P.7    Brimacombe, R.8
  • 55
    • 0021100296 scopus 로고
    • The Escherichia coli ribosomal protein L11 suppresses release factor 2 but promotes the release factor 1 activities in peptide chain termination
    • Tate WP, Schulze H, Nierhaus KH. 1983. The Escherichia coli ribosomal protein L11 suppresses release factor 2 but promotes the release factor 1 activities in peptide chain termination. J Biol Chem 258:12810-12815.
    • (1983) J Biol Chem , vol.258 , pp. 12810-12815
    • Tate, W.P.1    Schulze, H.2    Nierhaus, K.H.3
  • 56
    • 0030437751 scopus 로고    scopus 로고
    • Functional specificity of amino acid at position 246 in the tRNA mimicry domain of bacterial release factor 2
    • Uno M, Ito K, Nakamura Y. 1996. Functional specificity of amino acid at position 246 in the tRNA mimicry domain of bacterial release factor 2. Biochimie 78:935-943.
    • (1996) Biochimie , vol.78 , pp. 935-943
    • Uno, M.1    Ito, K.2    Nakamura, Y.3
  • 57
    • 0030013069 scopus 로고    scopus 로고
    • Loss of overproduction of polypeptide release factor 3 influences expression of the tryptophanase operon of Escherichia coli
    • Yanofsky C, Horn V, Nakamura Y. 1996. Loss of overproduction of polypeptide release factor 3 influences expression of the tryptophanase operon of Escherichia coli. J Bacteriol 178:3755-3762.
    • (1996) J Bacteriol , vol.178 , pp. 3755-3762
    • Yanofsky, C.1    Horn, V.2    Nakamura, Y.3
  • 58
    • 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, 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


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