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Volumn 37, Issue 6, 2003, Pages 931-943

Class-1 translation termination factors are functional analogs of aminoacyl-tRNAs

Author keywords

[No Author keywords available]

Indexed keywords

AMINOACYL TRANSFER RNA; NUCLEIC ACID; RIBOZYME; TRANSLATION TERMINATION FACTOR; TRANSLATION TERMINATION FACTOR RF1; TRANSLATION TERMINATION FACTOR RF2; UNCLASSIFIED DRUG;

EID: 2142816828     PISSN: 00268984     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (5)

References (75)
  • 1
    • 84918366244 scopus 로고
    • Peptide chain termination
    • Caskey C.T. 1980. Peptide chain termination. Trends Biochem. Sci. 5, 234-237.
    • (1980) Trends Biochem. Sci. , vol.5 , pp. 234-237
    • Caskey, C.T.1
  • 2
    • 0002965378 scopus 로고
    • TRNA-ribosome interactions
    • Eds Schimmel P.R., Soll D., Abelson J.U. Cold Spring Harbor, N.Y.: Cold Spring Harbor Laboratory Press
    • Cantor C.R. 1979. tRNA-ribosome interactions. In: Transfer RNA: Structure, Properties and Recognition. Eds Schimmel P.R., Soll D., Abelson J.U. Cold Spring Harbor, N.Y.: Cold Spring Harbor Laboratory Press, pp. 363-392.
    • (1979) Transfer RNA: Structure, Properties and Recognition , pp. 363-392
    • Cantor, C.R.1
  • 3
    • 0028305727 scopus 로고
    • A single proteolytic cleavage in release factor 2 stabilizes ribosome binding and abolishes peptidyl-tRNA hydrolysis activity
    • Moffat J.G., Tate W.P. 1994. A single proteolytic cleavage in release factor 2 stabilizes ribosome binding and abolishes peptidyl-tRNA hydrolysis activity. J. Biol. Chem. 269, 18899-18903.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18899-18903
    • Moffat, J.G.1    Tate, W.P.2
  • 4
    • 0027179715 scopus 로고
    • Mammalian polypeptide chain release factor and tryptophanyl-tRNA synthetase are distinct proteins
    • Frolova L., Dalphin M., Justesen J., Powell J., DrugeonG., Kisselev L., Tate W., Haenni A-L. 1993. Mammalian polypeptide chain release factor and tryptophanyl-tRNA synthetase are distinct proteins. EMBO J. 12, 4013-4019.
    • (1993) EMBO J. , vol.12 , pp. 4013-4019
    • Frolova, L.1    Dalphin, M.2    Justesen, J.3    Drugeong, P.J.4    Kisselev, L.5    Tate, W.6    Haenni, A.-L.7
  • 5
    • 0032473357 scopus 로고    scopus 로고
    • Mutations in RNAs of both ribosomal subunits cause defects in translation termination
    • Arkov A.L., Freistroffer D.V., Ehrenberg M., Murgola E.J. 1998. Mutations in RNAs of both ribosomal subunits cause defects in translation termination. EMBO J. 2, 1507-1514.
    • (1998) EMBO J. , vol.2 , pp. 1507-1514
    • Arkov, A.L.1    Freistroffer, D.V.2    Ehrenberg, M.3    Murgola, E.J.4
  • 6
    • 0033809290 scopus 로고    scopus 로고
    • Mutations in conserved regions of ribosomal RNAs decrease the productive association of peptide-chain release factors with the ribosome during translation termination
    • Arkov A.L., Freistroffer D.V., Pavlov M.Y., Ehrenberg M., Murgola E.J. 2000. Mutations in conserved regions of ribosomal RNAs decrease the productive association of peptide-chain release factors with the ribosome during translation termination. Biochimie. 82, 671-82.
    • (2000) Biochimie. , vol.82 , pp. 671-682
    • Arkov, A.L.1    Freistroffer, D.V.2    Pavlov, M.Y.3    Ehrenberg, M.4    Murgola, E.J.5
  • 7
    • 0035670709 scopus 로고    scopus 로고
    • A mechanism for stop codon recognition by the ribosome: A bioinformatics approach
    • Ivanov V., Beniaminov A., Mikheev A., Minyat E. 2001. A mechanism for stop codon recognition by the ribosome: a bioinformatics approach. RNA. 7, 1683-1692.
    • (2001) RNA , vol.7 , pp. 1683-1692
    • Ivanov, V.1    Beniaminov, A.2    Mikheev, A.3    Minyat, E.4
  • 8
    • 0034628438 scopus 로고    scopus 로고
    • A tripeptide 'anticodon' deciphers stop codons in messenger RNA
    • Ito K., Uno M., Nakamura Y. 2000. A tripeptide 'anticodon' deciphers stop codons in messenger RNA. Nature. 403, 680-684.
    • (2000) Nature , vol.403 , pp. 680-684
    • Ito, K.1    Uno, M.2    Nakamura, Y.3
  • 9
    • 0038012848 scopus 로고    scopus 로고
    • Mapping functionally important motifs SPF and GGQ of the decoding release factor RF2 to the Escherichia coli ribosome by hydroxyl radical footprinting. Implications for macromolecular mimicry and structural changes in RF2
    • Scarlett D.J., McCaughan K.K., Wilson D.N., Tate W.P. 2003. Mapping functionally important motifs SPF and GGQ of the decoding release factor RF2 to the Escherichia coli ribosome by hydroxyl radical footprinting. Implications for macromolecular mimicry and structural changes in RF2. J. Biol. Chem. 278, 5095-104.
    • (2003) J. Biol. Chem. , vol.278 , pp. 5095-5104
    • Scarlett, D.J.1    McCaughan, K.K.2    Wilson, D.N.3    Tate, W.P.4
  • 10
    • 0042737489 scopus 로고    scopus 로고
    • The ribosomal a site-bound sense and stop codons are similarly positioned towards the A1823-A1824 dinucleotide of the 18S ribosomal RNA
    • Bulygin K.N., Demeshkina A.N., Frolova L.Y., Graifer D.M., Ven'yaminova A.G., Kisselev L.L., Karpova G.G. 2003. The ribosomal A site-bound sense and stop codons are similarly positioned towards the A1823-A1824 dinucleotide of the 18S ribosomal RNA. FEBS Lett. 548, 97-102.
    • (2003) FEBS Lett. , vol.548 , pp. 97-102
    • Bulygin, K.N.1    Demeshkina, A.N.2    Frolova, L.Y.3    Graifer, D.M.4    Ven'yaminova, A.G.5    Kisselev, L.L.6    Karpova, G.G.7
  • 12
    • 0034860257 scopus 로고    scopus 로고
    • Stop codon recognition in ciliates: Euplotes release factor does not respond to reassigned UGA codon
    • Kervestin S., Frolova L., Kisselev L., Jean-Jean O. 2001. Stop codon recognition in ciliates: Euplotes release factor does not respond to reassigned UGA codon. EMBO Rep. 2, 680-684.
    • (2001) EMBO Rep. , vol.2 , pp. 680-684
    • Kervestin, S.1    Frolova, L.2    Kisselev, L.3    Jean-Jean, O.4
  • 13
    • 0037173091 scopus 로고    scopus 로고
    • Omnipotent decoding potential resides in eukaryotic translation termination factor eRF1 of variant-code organisms and is modulated by the interactions of amino acid sequences within the domain 1
    • Ito K., Frolova L., Seit-Nebi A., Karamyshev A., Kisselev L., Nakamura Y. 2002. Omnipotent decoding potential resides in eukaryotic translation termination factor eRF1 of variant-code organisms and is modulated by the interactions of amino acid sequences within the domain 1. Proc. Natl. Acad. Sci. USA. 99, 8494-8499.
    • (2002) Proc. Natl. Acad. Sci. USA. , vol.99 , pp. 8494-8499
    • Ito, K.1    Frolova, L.2    Seit-Nebi, A.3    Karamyshev, A.4    Kisselev, L.5    Nakamura, Y.6
  • 14
    • 0029975504 scopus 로고    scopus 로고
    • Conserved motifs in prokaryotic and eukaryotic polypeptide release factors: TRNA-protein mimicry hypothesis
    • Ito K., Ebihara K., Uno M., Nakamura Y. 1996. Conserved motifs in prokaryotic and eukaryotic polypeptide release factors: tRNA-protein mimicry hypothesis. Proc. Natl. Acad. Sci. USA. 93, 5443-5448.
    • (1996) Proc. Natl. Acad. Sci. USA. , vol.93 , pp. 5443-5448
    • Ito, K.1    Ebihara, K.2    Uno, M.3    Nakamura, Y.4
  • 15
    • 33747374668 scopus 로고    scopus 로고
    • Russian source
  • 16
    • 0034603210 scopus 로고    scopus 로고
    • The crystal structure of human eukaryotic release factor eRF1-mechanism of stop codon recognition and peptidyl-tRNA hydrolysis
    • Song H., Mugnier P., Das A.K., Webb H.M., Evans D.R., Tuite M.F., Hemmings B.A., Barford D. 2000. The crystal structure of human eukaryotic release factor eRF1-mechanism of stop codon recognition and peptidyl-tRNA hydrolysis. Cell. 100, 311-321.
    • (2000) Cell , vol.100 , pp. 311-321
    • Song, H.1    Mugnier, P.2    Das, A.K.3    Webb, H.M.4    Evans, D.R.5    Tuite, M.F.6    Hemmings, B.A.7    Barford, D.8
  • 17
    • 0032840382 scopus 로고    scopus 로고
    • Mutations in the highly conserved GGQ motif of class 1 polypeptide release factors abolish ability of human eRF1 to trigger peptidyl-tRNA hydrolysis
    • Frolova L.Y., Tsivkovskii R.Y., Sivolobova G.F., Oparina N. Y., Serpinsky O.I., Blinov V.M., Tatkov S.I., Kisselev L.L. 1999. Mutations in the highly conserved GGQ motif of class 1 polypeptide release factors abolish ability of human eRF1 to trigger peptidyl-tRNA hydrolysis. RNA. 5, 1014-20.
    • (1999) RNA , vol.5 , pp. 1014-1020
    • Frolova, L.Y.1    Tsivkovskii, R.Y.2    Sivolobova, G.F.3    Oparina, N.Y.4    Serpinsky, O.I.5    Blinov, V.M.6    Tatkov, S.I.7    Kisselev, L.L.8
  • 21
    • 0036810254 scopus 로고    scopus 로고
    • Release of peptide promoted by the GGQ-motif of class-1 release factors regulates the GTPase activity of RF3
    • Zavialov A.V., Mora L., Buckingham R.H., Ehrenberg M. 2002. Release of peptide promoted by the GGQ-motif of class-1 release factors regulates the GTPase activity of RF3. Mol. Cell. 10, 789-798.
    • (2002) Mol. Cell. , vol.10 , pp. 789-798
    • Zavialov, A.V.1    Mora, L.2    Buckingham, R.H.3    Ehrenberg, M.4
  • 22
    • 0037223622 scopus 로고    scopus 로고
    • The essential role of the invariant GGQ motif in the function and the stability in vivo of bacterial release factors RF1 and RF2
    • Mora L., Heurgue-Hamard V., Champ S., Ehrenberg M., Kisselev L.I., Buckingham R.H. 2003. The essential role of the invariant GGQ motif in the function and the stability in vivo of bacterial release factors RF1 and RF2. Mol. Microbiol. 47, 267-275.
    • (2003) Mol. Microbiol. , vol.47 , pp. 267-275
    • Mora, L.1    Heurgue-Hamard, V.2    Champ, S.3    Ehrenberg, M.4    Kisselev, L.I.5    Buckingham, R.H.6
  • 23
    • 0034725103 scopus 로고    scopus 로고
    • Translation termination factor aRF1 from the archaeon Methanococcus jannaschii is active with eukaryotic ribosomes
    • Dontsova M., Frolova L., Vassilieva J., Piendl W., Kisselev L., Garber M. 2000. Translation termination factor aRF1 from the archaeon Methanococcus jannaschii is active with eukaryotic ribosomes. FEBS Lett. 472, 213-216.
    • (2000) FEBS Lett. , vol.472 , pp. 213-216
    • Dontsova, M.1    Frolova, L.2    Vassilieva, J.3    Piendl, W.4    Kisselev, L.5    Garber, M.6
  • 24
    • 33747352057 scopus 로고    scopus 로고
    • Russian source
  • 25
    • 0035476654 scopus 로고    scopus 로고
    • Class-1 translation termination factors: Invariant GGQ minidomain is essential for release activity and ribosome binding but not for stop codon recognition
    • Seit-Nebi A., Frolova L., Justesen J., Kisselev L. 2001. Class-1 translation termination factors: invariant GGQ minidomain is essential for release activity and ribosome binding but not for stop codon recognition. Nucl. Acids. Res. 29, 3982-3987.
    • (2001) Nucl. Acids. Res. , vol.29 , pp. 3982-3987
    • Seit-Nebi, A.1    Frolova, L.2    Justesen, J.3    Kisselev, L.4
  • 26
    • 0037084101 scopus 로고    scopus 로고
    • The hemK gene in Escherichia coli encodes the N5-glutamine methyltransferase that modifies peptide release factors
    • Heurgue-Hamard V., Champ S., Engstrom A., Ehrenberg M., Buckingham R.H. 2002. The hemK gene in Escherichia coli encodes the N5-glutamine methyltransferase that modifies peptide release factors. EMBO J. 21, 769-780.
    • (2002) EMBO J. , vol.21 , pp. 769-780
    • Heurgue-Hamard, V.1    Champ, S.2    Engstrom, A.3    Ehrenberg, M.4    Buckingham, R.H.5
  • 27
    • 0034672060 scopus 로고    scopus 로고
    • A post-translational modification in the GGQ motif of RF2 from Escherichia coli stimulates termination of translation
    • Dinchas-Rundquist V., Engstrom A., Mora L., Heurgue-Hamard V., Buckingham R.H., Ehrenberg M. 2000. A post-translational modification in the GGQ motif of RF2 from Escherichia coli stimulates termination of translation. EMBO J. 19, 6900-6907.
    • (2000) EMBO J. , vol.19 , pp. 6900-6907
    • Dinchas-Rundquist, V.1    Engstrom, A.2    Mora, L.3    Heurgue-Hamard, V.4    Buckingham, R.H.5    Ehrenberg, M.6
  • 28
    • 0030437751 scopus 로고    scopus 로고
    • Functional specificity of amino acid at position 246 in the RNA mimicry domain of bacterial release factor 2
    • Uno M., Ito K., Nakamura Y. 1996. Functional specificity of amino acid at position 246 in the RNA 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
  • 29
    • 0001105070 scopus 로고    scopus 로고
    • Genetic probes to bacterial release factors: TRNA mimicry hypothesis and beyond
    • Garrett R.A., Douthwaite S.R., Lilias A., Mathesson A.T., Moore P.B., Noller H.F., Eds. Washington, DC: ASM Press
    • Nakamura Y., Kawazu Y., Uno M., Yoshimura K., Ito K. 2000. Genetic probes to bacterial release factors: tRNA mimicry hypothesis and beyond. In: Garrett R.A., Douthwaite S.R., Lilias A., Mathesson A.T., Moore P.B., Noller H.F., Eds. The ribosome: structure, function, antibiotics, and cellular interactions. Washington, DC: ASM Press, pp. 519-526.
    • (2000) The Ribosome: Structure, Function, Antibiotics, and Cellular Interactions , pp. 519-526
    • Nakamura, Y.1    Kawazu, Y.2    Uno, M.3    Yoshimura, K.4    Ito, K.5
  • 30
    • 0034548165 scopus 로고    scopus 로고
    • The ribosomal binding and peptidyl-tRNA hydrolysis functions of Escherichia coli release factor 2 are linked through residue 246
    • Wilson D.N., Guevremont D., Tate W.P. 2000. The ribosomal binding and peptidyl-tRNA hydrolysis functions of Escherichia coli release factor 2 are linked through residue 246. RNA. 6, 1704-17013.
    • (2000) RNA , vol.6 , pp. 1704-17013
    • Wilson, D.N.1    Guevremont, D.2    Tate, W.P.3
  • 31
    • 0034618493 scopus 로고    scopus 로고
    • Release factors and their role as decoding proteins: Specificity and fidelity for termination of protein synthesis
    • Poole E., Tate W. 2000. Release factors and their role as decoding proteins: specificity and fidelity for termination of protein synthesis. Biochim. Biophys. Acta. 1493, 1-11.
    • (2000) Biochim. Biophys. Acta. , vol.1493 , pp. 1-11
    • Poole, E.1    Tate, W.2
  • 33
    • 0034826629 scopus 로고    scopus 로고
    • The polypeptide chain release factor eRF1 specifically contacts the s4.UGA stop codon located in the a site of eukaryotic ribosomes
    • Chavatte L., Frolova L., Kisselev L., Favre A. 2001. The polypeptide chain release factor eRF1 specifically contacts the s4.UGA stop codon located in the A site of eukaryotic ribosomes. Eur. J. Biochem. 268, 2896-2904.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 2896-2904
    • Chavatte, L.1    Frolova, L.2    Kisselev, L.3    Favre, A.4
  • 34
    • 0036792666 scopus 로고    scopus 로고
    • The invariant uridine of stop codons contacts the conserved NIKSR loop of human eRF1 in the ribosome
    • Chavatte L., Seit-Nebi A., Dubovaya V., Havre A. 2002. The invariant uridine of stop codons contacts the conserved NIKSR loop of human eRF1 in the ribosome. MBO J. 21, 5302-5311.
    • (2002) MBO J. , vol.21 , pp. 5302-5311
    • Chavatte, L.1    Seit-Nebi, A.2    Dubovaya, V.3    Havre, A.4
  • 35
    • 0037029087 scopus 로고    scopus 로고
    • Positioning of the mRNA stop signal with respect to polypeptide chain release factors and ribosomal proteins in 80S ribosomes
    • Bulygin K.N., Repkova M.N, Ven'yaminova A.G., Graifer D.M., Karpova G.G., Frolova L.Yu., Kisselev L.L. 2002. Positioning of the mRNA stop signal with respect to polypeptide chain release factors and ribosomal proteins in 80S ribosomes. FEBS Lett. 514, 96-101.
    • (2002) FEBS Lett. , vol.514 , pp. 96-101
    • Bulygin, K.N.1    Repkova, M.N.2    Ven'Yaminova, A.G.3    Graifer, D.M.4    Karpova, G.G.5    Frolova, L.Yu.6    Kisselev, L.L.7
  • 36
    • 0037029037 scopus 로고    scopus 로고
    • A tripeptide discriminator for stop codon recognition
    • Nakamura Y., Ito K. 2002. A tripeptide discriminator for stop codon recognition. FEBS Lett. 514, 30-33.
    • (2002) FEBS Lett. , vol.514 , pp. 30-33
    • Nakamura, Y.1    Ito, K.2
  • 37
    • 0034640086 scopus 로고    scopus 로고
    • Mimicry grasps reality in translation termination
    • Nakamura Y., Ito K., Ehrenberg M. 2000. Mimicry grasps reality in translation termination. Cell. 101, 349-352.
    • (2000) Cell , vol.101 , pp. 349-352
    • Nakamura, Y.1    Ito, K.2    Ehrenberg, M.3
  • 38
    • 0037439231 scopus 로고    scopus 로고
    • Termination of translation: Interplay of mRNA, rRNAs and release factors
    • Kisselev L.L., Ehrenberg M., Frolova L.Yu. 2003. Termination of translation: interplay of mRNA, rRNAs and release factors. EMBO J. 22, 175-182.
    • (2003) EMBO J. , vol.22 , pp. 175-182
    • Kisselev, L.L.1    Ehrenberg, M.2    Frolova, L.Yu.3
  • 39
    • 0037310005 scopus 로고    scopus 로고
    • Making sense of mimic in translation termination
    • Nakamura Y., Ito K. 2003. Making sense of mimic in translation termination. Trends Biochem. Sci. 28, 99-105.
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 99-105
    • Nakamura, Y.1    Ito, K.2
  • 40
    • 0036216442 scopus 로고    scopus 로고
    • Highly conserved NIKS tetrapeptide is functionally essential in eukaryotic translation termination factor eRF1
    • Frolova L., Seit-Nebi A., Kisselev L. 2002. Highly conserved NIKS tetrapeptide is functionally essential in eukaryotic translation termination factor eRF1. RNA. 8, 129-136.
    • (2002) RNA , vol.8 , pp. 129-136
    • Frolova, L.1    Seit-Nebi, A.2    Kisselev, L.3
  • 41
    • 0036747332 scopus 로고    scopus 로고
    • Conversion of omnipotent translation termination factor eRF1 into ciliate-like UGA-only unipotent eRF1
    • Seit-Nebi A., Frolova L., Kisselev L. 2002. Conversion of omnipotent translation termination factor eRF1 into ciliate-like UGA-only unipotent eRF1. EMBO Rep. 3, 881-886.
    • (2002) EMBO Rep. , vol.3 , pp. 881-886
    • Seit-Nebi, A.1    Frolova, L.2    Kisselev, L.3
  • 42
    • 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
  • 43
    • 0034069537 scopus 로고    scopus 로고
    • Translation termination in eukaryotes: Polypeptide release factor eRF1 is composed of functionally and structurally distinct domains
    • Frolova L.Y., Merkulova T.I., Kisselev L.L. 2000. Translation termination in eukaryotes: polypeptide release factor eRF1 is composed of functionally and structurally distinct domains. RNA. 6, 381-390.
    • (2000) RNA , vol.6 , pp. 381-390
    • Frolova, L.Y.1    Merkulova, T.I.2    Kisselev, L.L.3
  • 44
    • 0033784538 scopus 로고    scopus 로고
    • Functional sites of interaction between release factor RF1 and the ribosome
    • Wilson K.S., Ito K., Noller H.F., Nakamura Y. 2000. Functional sites of interaction between release factor RF1 and the ribosome. Nature Struct. Biol. 7, 866-870.
    • (2000) Nature Struct. Biol. , vol.7 , pp. 866-870
    • Wilson, K.S.1    Ito, K.2    Noller, H.F.3    Nakamura, Y.4
  • 46
    • 0021334017 scopus 로고
    • A temperature-sensitive mutant of Escherichia coli that shows enhanced misreading of UAG/A and increased efficiency for some tRNA nonsense suppressors
    • Ryden S.M., Isaksson L.A. 1984. A temperature-sensitive mutant of Escherichia coli that shows enhanced misreading of UAG/A and increased efficiency for some tRNA nonsense suppressors. Mol. Gen. Genet. 193, 38-45.
    • (1984) Mol. Gen. Genet. , vol.193 , pp. 38-45
    • Ryden, S.M.1    Isaksson, L.A.2
  • 47
    • 0025734136 scopus 로고
    • Salmonella typhimurium prfA mutants defective in release factor 1
    • Elliott T., Wang X. 1991. Salmonella typhimurium prfA mutants defective in release factor 1. J Bacteriol. 173, 4144-4154.
    • (1991) J Bacteriol. , vol.173 , pp. 4144-4154
    • Elliott, T.1    Wang, X.2
  • 48
    • 0030872684 scopus 로고    scopus 로고
    • Eukaryotic release factor 1 eRF1. abolishes readthrough and competes with suppressor tRNAs at all three termination codons in messenger RNA
    • Drugeon G., Jean-Jean O., Frolova L., Le Goff X., Philippe M., Kisselev L., Haenni A.L. 1997. Eukaryotic release factor 1 eRF1. abolishes readthrough and competes with suppressor tRNAs at all three termination codons in messenger RNA. Nucl. Acids Res. 25, 2254-2258.
    • (1997) Nucl. Acids Res. , vol.25 , pp. 2254-2258
    • Drugeon, G.1    Jean-Jean, O.2    Frolova, L.3    Le Goff, X.4    Philippe, M.5    Kisselev, L.6    Haenni, A.L.7
  • 49
    • 0033040888 scopus 로고    scopus 로고
    • Amber UAG suppressors affected in UGA/UAA-specific polypeptide release factor 2 of bacteria: Genetic prediction of initial binding to ribosome preceding stop codon recognition
    • Yoshimura K., Ito K., Nakamura Y. 1999. Amber UAG suppressors affected in UGA/UAA-specific polypeptide release factor 2 of bacteria: genetic prediction of initial binding to ribosome preceding stop codon recognition. Genes Cells. 4, 253-266.
    • (1999) Genes Cells , vol.4 , pp. 253-266
    • Yoshimura, K.1    Ito, K.2    Nakamura, Y.3
  • 50
    • 19244364778 scopus 로고    scopus 로고
    • Eukaryotic polypeptide chain release factor eRF3 is an eRF1- and ribosome-dependent guanosine triphosphatase
    • Frolova L., Le Goff 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    Le Goff, X.2    Zhouravleva, G.3    Davydova, E.4    Philippe, M.5    Kisselev, L.6
  • 51
    • 0043168057 scopus 로고    scopus 로고
    • Stop codons and UGG promote efficient binding of the human polypeptide release factor eRF1 to the eukaryotic ribosomal a site
    • Chavatte L., Frolova L., Laugâa P., Kisselev L., Favre A. 2003. Stop codons and UGG promote efficient binding of the human polypeptide release factor eRF1 to the eukaryotic ribosomal A site. J. Mol. Biol. 331, 745-758.
    • (2003) J. Mol. Biol. , vol.331 , pp. 745-758
    • Chavatte, L.1    Frolova, L.2    Laugâa, P.3    Kisselev, L.4    Favre, A.5
  • 52
    • 0035252889 scopus 로고    scopus 로고
    • Ribosome fidelity: TRNA discrimination, proofreading and induced fit
    • Rodnina M.V., Wintermeyer W. 2001. Ribosome fidelity: tRNA discrimination, proofreading and induced fit. Trends Biochem. Sci. 26, 124-130.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 124-130
    • Rodnina, M.V.1    Wintermeyer, W.2
  • 54
    • 0037378170 scopus 로고    scopus 로고
    • A twisted tRNA intermediate sets the threshold for decoding
    • Yarus M., Valle M., Frank J. 2003. A twisted tRNA intermediate sets the threshold for decoding. RNA. 9, 384-385.
    • (2003) RNA , vol.9 , pp. 384-385
    • Yarus, M.1    Valle, M.2    Frank, J.3
  • 55
    • 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
  • 58
    • 0032493451 scopus 로고    scopus 로고
    • Single amino acid substitution in prokaryote polypeptide release factor 2 permits it to terminate translation at all three stop codons
    • Ito K., Uno M., Nakamura Y. 1998. Single amino acid substitution in prokaryote polypeptide release factor 2 permits it to terminate translation at all three stop codons. Proc. Natl. Acad. Sci. USA. 95, 8165-8169.
    • (1998) Proc. Natl. Acad. Sci. USA. , vol.95 , pp. 8165-8169
    • Ito, K.1    Uno, M.2    Nakamura, Y.3
  • 59
    • 0032969177 scopus 로고    scopus 로고
    • C-terminal domains of human translation termination factors eRF1 and eRF3 mediate their in vivo interaction
    • Merkulova T.I., Frolova L.Y., Lazar M., Camonis J., Kisselev L.L. 1999. C-terminal domains of human translation termination factors eRF1 and eRF3 mediate their in vivo interaction. FEBS Lett. 443, 41-47.
    • (1999) FEBS Lett. , vol.443 , pp. 41-47
    • Merkulova, T.I.1    Frolova, L.Y.2    Lazar, M.3    Camonis, J.4    Kisselev, L.L.5
  • 60
    • 0033016754 scopus 로고    scopus 로고
    • C-terminal interaction of translational release factors eRF1 and eRF3 of fission yeast: G-domain uncoupled binding and the role of conserved amino acids
    • Ebihara K., Nakamura Y. 1999. C-terminal interaction of translational release factors eRF1 and eRF3 of fission yeast: G-domain uncoupled binding and the role of conserved amino acids. RNA. 5, 739-750.
    • (1999) RNA , vol.5 , pp. 739-750
    • Ebihara, K.1    Nakamura, Y.2
  • 61
    • 0032937983 scopus 로고    scopus 로고
    • The C-terminus of eRF1 defines a functionally important domain for translation termination in Saccharomyces cerevisiae
    • Eurwilaichitr L., Graves F., Stansfield I., Tuite M.F. 1999. The C-terminus of eRF1 defines a functionally important domain for translation termination in Saccharomyces cerevisiae. Mol. Microbiol. 323, 485-496.
    • (1999) Mol. Microbiol. , vol.323 , pp. 485-496
    • Eurwilaichitr, L.1    Graves, F.2    Stansfield, I.3    Tuite, M.F.4
  • 63
    • 0035812714 scopus 로고    scopus 로고
    • A post-termination ribosomal complex is the guanine nucleotide exchange factor for peptide release factor RF3
    • Zavialov A.V., Buckingham R.H., Ehrenberg M. 2001. A post-termination ribosomal complex is the guanine nucleotide exchange factor for peptide release factor RF3. Cell. 107, 115-124.
    • (2001) Cell , vol.107 , pp. 115-124
    • Zavialov, A.V.1    Buckingham, R.H.2    Ehrenberg, M.3
  • 64
    • 0347517767 scopus 로고    scopus 로고
    • Stop codon recognition and interaction with peptide release factor RF3 of truncated and chimeric RF1 and RF2 from E.coli
    • in press
    • Mora L., Zavialov A., Ehrenberg M., Buckingham R. 2003. Stop codon recognition and interaction with peptide release factor RF3 of truncated and chimeric RF1 and RF2 from E.coli. Mol. Microbiol. in press.
    • (2003) Mol. Microbiol.
    • Mora, L.1    Zavialov, A.2    Ehrenberg, M.3    Buckingham, R.4
  • 65
    • 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.V., Pavlov M.Y., MacDougall J., Buckingham R.H., 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. EMBOJ. 16, 4126-4133.
    • (1997) EMBOJ , vol.16 , pp. 4126-4133
    • Freistroffer, D.V.1    Pavlov, M.Y.2    MacDougall, J.3    Buckingham, R.H.4    Ehrenberg, M.5
  • 67
    • 0037245660 scopus 로고    scopus 로고
    • The critical role of the universally conserved A2602 of 23S ribosomal RNA in the release of the nascent peptide during translation termination
    • Polacek N., Gomez M.J., Ito K., Xiong L., Nakamura Y., Mankin A. 2003. The critical role of the universally conserved A2602 of 23S ribosomal RNA in the release of the nascent peptide during translation termination. Mol. Cell. 11, 103-112.
    • (2003) Mol. Cell. , vol.11 , pp. 103-112
    • Polacek, N.1    Gomez, M.J.2    Ito, K.3    Xiong, L.4    Nakamura, Y.5    Mankin, A.6
  • 70
    • 0030592511 scopus 로고    scopus 로고
    • Emerging understanding of translation termination
    • Nakamura Y., Ito K., 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
  • 71
    • 0033579365 scopus 로고    scopus 로고
    • Crystal structure of Thermotoga maritima ribosome recycling factor: A tRNA mimic
    • Selmer M., Al-Karadaghi S., Hirokawa G., Kaji A., Liljas A. 1999. Crystal structure of Thermotoga maritima ribosome recycling factor: a tRNA mimic. Science. 286, 2349-2352.
    • (1999) Science , vol.286 , pp. 2349-2352
    • Selmer, M.1    Al-Karadaghi, S.2    Hirokawa, G.3    Kaji, A.4    Liljas, A.5
  • 72
    • 0343618468 scopus 로고    scopus 로고
    • Crystal structure of the ribosome recycling factor from Escherichia coli
    • Kim K.K., Min K., Suh S.W. 2000. Crystal structure of the ribosome recycling factor from Escherichia coli. EMBO J. 19, 2362-2370.
    • (2000) EMBO J , vol.19 , pp. 2362-2370
    • Kim, K.K.1    Min, K.2    Suh, S.W.3
  • 74
    • 0033751564 scopus 로고    scopus 로고
    • Crystal structure combined with genetic analysis of the Thermus thermophilus ribosome recycling factor shows that a flexible hinge may act as afunctional switch
    • Toyoda T., Tin O.F., Ito K., Fujiwara T., Kumasaka T., Yamamoto M., Garber M.B., Nakamura Y. 2000. Crystal structure combined with genetic analysis of the Thermus thermophilus ribosome recycling factor shows that a flexible hinge may act as afunctional switch. RNA. 6, 1432-1444.
    • (2000) RNA , vol.6 , pp. 1432-1444
    • Toyoda, T.1    Tin, O.F.2    Ito, K.3    Fujiwara, T.4    Kumasaka, T.5    Yamamoto, M.6    Garber, M.B.7    Nakamura, Y.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.