메뉴 건너뛰기




Volumn 16, Issue 8, 2010, Pages 1623-1633

The codon specificity of eubacterial release factors is determined by the sequence and size of the recognition loop

Author keywords

Codon recognition; Codon specificity; Release factor; Stop codon; Translation

Indexed keywords

MITOCHONDRIAL PROTEIN; PROTEIN MRF1; PROTEIN MRF2; UNCLASSIFIED DRUG;

EID: 77955113186     PISSN: 13558382     EISSN: 14699001     Source Type: Journal    
DOI: 10.1261/rna.2117010     Document Type: Article
Times cited : (10)

References (43)
  • 2
    • 0032246224 scopus 로고    scopus 로고
    • The analysis of translational activity using a reporter gene constructed from repeats of an antibody-binding domain from protein A
    • Bjornsson A, Mottagui-Tabar S, Isaksson LA. 1998. The analysis of translational activity using a reporter gene constructed from repeats of an antibody-binding domain from protein A. Methods Mol Biol 77: 75-91.
    • (1998) Methods Mol Biol , vol.77 , pp. 75-91
    • Bjornsson, A.1    Mottagui-Tabar, S.2    Isaksson, L.A.3
  • 4
    • 0017606476 scopus 로고
    • Genetic studies of the lac repressor. III. Additional correlation of mutational sites with specific amino acid residues
    • Coulondre C, Miller JH. 1977. Genetic studies of the lac repressor. III. Additional correlation of mutational sites with specific amino acid residues. J Mol Biol 117: 525-567. (Pubitemid 8256690)
    • (1977) Journal of Molecular Biology , vol.117 , Issue.3 , pp. 525-567
    • Coulondre, C.1    Miller, J.H.2
  • 5
    • 70449209123 scopus 로고
    • On protein synthesis
    • Crick FH. 1958. On protein synthesis. Symp Soc Exp Biol 12: 138-163.
    • (1958) Symp Soc Exp Biol , vol.12 , pp. 138-163
    • Crick, F.H.1
  • 6
    • 33645801951 scopus 로고    scopus 로고
    • Comparison of characteristics and function of translation termination signals between and within prokaryotic and eukaryotic organisms
    • Cridge AG, Major LL, Mahagaonkar AA, Poole ES, Isaksson LA, Tate WP. 2006. Comparison of characteristics and function of translation termination signals between and within prokaryotic and eukaryotic organisms. Nucleic Acids Res 34: 1959-1973.
    • (2006) Nucleic Acids Res , vol.34 , pp. 1959-1973
    • Cridge, A.G.1    Major, L.L.2    Mahagaonkar, A.A.3    Poole, E.S.4    Isaksson, L.A.5    Tate, W.P.6
  • 7
    • 27944508307 scopus 로고    scopus 로고
    • Amino acid specificity in translation
    • Dale T, Uhlenbeck OC. 2005. Amino acid specificity in translation. Trends Biochem Sci 30: 659-665.
    • (2005) Trends Biochem Sci , vol.30 , pp. 659-665
    • Dale, T.1    Uhlenbeck, O.C.2
  • 11
    • 0020959710 scopus 로고
    • Studies on transformation of Escherichia coli with plasmids
    • Hanahan D. 1983. Studies on transformation of Escherichia coli with plasmids. J Mol Biol 166: 557-580. (Pubitemid 13027898)
    • (1983) Journal of Molecular Biology , vol.166 , Issue.4 , pp. 557-580
    • Hanahan, D.1
  • 12
    • 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 95: 8165-8169.
    • (1998) Proc Natl Acad Sci , vol.95 , pp. 8165-8169
    • Ito, K.1    Uno, M.2    Nakamura, Y.3
  • 13
    • 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
  • 14
  • 17
    • 46149104347 scopus 로고    scopus 로고
    • Different aa-tRNAs Are Selected Uniformly on the Ribosome
    • DOI 10.1016/j.molcel.2008.04.026, PII S1097276508003353
    • Ledoux S, Uhlenbeck OC. 2008. Different aa-tRNAs are selected uniformly on the ribosome. Mol Cell 31: 114-123. (Pubitemid 351905919)
    • (2008) Molecular Cell , vol.31 , Issue.1 , pp. 114-123
    • Ledoux, S.1    Uhlenbeck, O.C.2
  • 18
    • 0037126612 scopus 로고    scopus 로고
    • Sec decoding UGA at the recoding site of Escherichia coli formate dehydrogenase H
    • Sec decoding UGA at the recoding site of Escherichia coli formate dehydrogenase H. EMBO J 20: 7284-7293.
    • (2001) EMBO J , vol.20 , pp. 7284-7293
    • Mansell, J.B.1    Guevremont, D.2    Poole, E.S.3    Tate, W.P.4
  • 20
    • 0347517767 scopus 로고    scopus 로고
    • Stop codon recognition and interactions with peptide release factor RF3 of truncated and chimeric RF1 and RF2 from Escherichia coli
    • DOI 10.1046/j.1365-2958.2003.03799.x
    • Mora L, Zavialov A, Ehrenberg M, Buckingham RH. 2003. Stop codon recognition and interactions with peptide release factor RF3 of truncated and chimeric RF1 and RF2 from Escherichia coli. Mol Microbiol 50: 1467-1476. (Pubitemid 38010445)
    • (2003) Molecular Microbiology , vol.50 , Issue.5 , pp. 1467-1476
    • Mora, L.1    Zavialov, A.2    Ehrenberg, M.3    Buckingham, R.H.4
  • 21
    • 0028175762 scopus 로고
    • The second to last amino acid in the nascent peptide as a codon context determinant
    • Mottagui-Tabar S, Bjornsson A, Isaksson LA. 1994. The second to last amino acid in the nascent peptide as a codon context determinant. EMBO J 13: 249-257.
    • (1994) EMBO J , vol.13 , pp. 249-257
    • Mottagui-Tabar, S.1    Bjornsson, A.2    Isaksson, L.A.3
  • 22
    • 0037029037 scopus 로고    scopus 로고
    • A tripeptide discriminator for stop codon recognition
    • DOI 10.1016/S0014-5793(02)02330-X, PII S001457930202330X
    • Nakamura Y, Ito K. 2002. A tripeptide discriminator for stop codon recognition. FEBS Lett 514: 30-33. (Pubitemid 34251237)
    • (2002) FEBS Letters , vol.514 , Issue.1 , pp. 30-33
    • Nakamura, Y.1    Ito, K.2
  • 24
    • 0026573893 scopus 로고
    • The mitochondrial genomes of two nematodes, Caenorhabditis elegans and Ascaris suum
    • Okimoto R, Macfarlane JL, Clary DO, Wolstenholme DR. 1992. The mitochondrial genomes of two nematodes, Caenorhabditis elegans and Ascaris suum. Genetics 130: 471-498.
    • (1992) Genetics , vol.130 , pp. 471-498
    • Okimoto, R.1    Macfarlane, J.L.2    Clary, D.O.3    Wolstenholme, D.R.4
  • 25
    • 24944507742 scopus 로고    scopus 로고
    • Common and specific amino acid residues in the prokaryotic polypeptide release factors RF1 and RF2: Possible functional implications
    • Oparina NJ, Kalinina OV, Gelfand MS, Kisselev LL. 2005. Common and specific amino acid residues in the prokaryotic polypeptide release factors RF1 and RF2: Possible functional implications. Nucleic Acids Res 33: 5226-5234.
    • (2005) Nucleic Acids Res , vol.33 , pp. 5226-5234
    • Oparina, N.J.1    Kalinina, O.V.2    Gelfand, M.S.3    Kisselev, L.L.4
  • 26
    • 0026674036 scopus 로고
    • Sequence comparison of new prokaryotic and mitochondrial members of the polypeptide chain release factor family predicts a five-domain model for release factor structure
    • Pel HJ, Rep M, Grivell LA. 1992. Sequence comparison of new prokaryotic and mitochondrial members of the polypeptide chain release factor family predicts a five-domain model for release factor structure. Nucleic Acids Res 20: 4423-4428.
    • (1992) Nucleic Acids Res , vol.20 , pp. 4423-4428
    • Pel, H.J.1    Rep, M.2    Grivell, L.A.3
  • 29
    • 34547226652 scopus 로고    scopus 로고
    • Accommodating the bacterial decoding release factor as an alien protein among the RNAs at the active site of the ribosome
    • Poole ES, Young DJ, Askarian-Amiri ME, Scarlett DJ, Tate WP. 2007. Accommodating the bacterial decoding release factor as an alien protein among the RNAs at the active site of the ribosome. Cell Res 17: 591-607.
    • (2007) Cell Res , vol.17 , pp. 591-607
    • Poole, E.S.1    Young, D.J.2    Askarian-Amiri, M.E.3    Scarlett, D.J.4    Tate, W.P.5
  • 30
    • 0025325983 scopus 로고
    • The megaprimer method of site-directed mutagenesis
    • Sarkar G, Sommer SS. 1990. The 'megaprimer' method of site-directed mutagenesis. Biotechniques 8: 404-407.
    • (1990) Biotechniques , vol.8 , pp. 404-407
    • Sarkar, G.1    Sommer, S.S.2
  • 31
    • 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 DJ, McCaughan KK, Wilson DN, Tate WP. 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: 15095-15104.
    • (2003) J Biol Chem , vol.278 , pp. 15095-15104
    • Scarlett, D.J.1    McCaughan, K.K.2    Wilson, D.N.3    Tate, W.P.4
  • 33
    • 4143064788 scopus 로고    scopus 로고
    • Structural analyses of peptide release factor 1 from Thermotoga maritima reveal domain flexibility required for its interaction with the ribosome
    • DOI 10.1016/j.jmb.2004.05.055, PII S0022283604006321
    • Shin DH, Brandsen J, Jancarik J, Yokota H, Kim R, Kim SH. 2004. Structural analyses of peptide release factor 1 from Thermotoga maritima reveal domain flexibility required for its interaction with the ribosome. J Mol Biol 341: 227-239. (Pubitemid 39090647)
    • (2004) Journal of Molecular Biology , vol.341 , Issue.1 , pp. 227-239
    • Shin, D.H.1    Brandsen, J.2    Jancarik, J.3    Yokota, H.4    Kim, R.5    Kim, S.-H.6
  • 35
  • 36
    • 0030437751 scopus 로고    scopus 로고
    • Functional specificity of amino acid at position 246 in the tRNA mimicry domain of bacterial release factor 2
    • DOI 10.1016/S0300-9084(97)86715-6
    • 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. (Pubitemid 27193112)
    • (1996) Biochimie , vol.78 , Issue.11-12 , pp. 935-943
    • Uno, M.1    Ito, K.2    Nakamura, Y.3
  • 37
    • 0037133246 scopus 로고    scopus 로고
    • Polypeptide release at sense and noncognate stop codons by localized charge-exchange alterations in translational release factors
    • Uno M, Ito K, Nakamura Y. 2002. Polypeptide release at sense and noncognate stop codons by localized charge-exchange alterations in translational release factors. Proc Natl Acad Sci 99: 1819-1824.
    • (2002) Proc Natl Acad Sci , vol.99 , pp. 1819-1824
    • Uno, M.1    Ito, K.2    Nakamura, Y.3
  • 38
    • 0035697089 scopus 로고    scopus 로고
    • Bacterial polypeptide release factor RF2 is structurally distinct from eukaryotic eRF1
    • DOI 10.1016/S1097-2765(01)00415-4
    • Vestergaard B, Van LB, Andersen GR, Nyborg J, Buckingham RH, Kjeldgaard M. 2001. Bacterial polypeptide release factor RF2 is structurally distinct from eukaryotic eRF1. Mol Cell 8: 1375-1382. (Pubitemid 34085006)
    • (2001) Molecular Cell , vol.8 , Issue.6 , pp. 1375-1382
    • Vestergaard, B.1    Van, L.B.2    Andersen, G.R.3    Nyborg, J.4    Buckingham, R.H.5    Kjeldgaard, M.6
  • 40
    • 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 DN, Guevremont D, Tate WP. 2000. The ribosomal binding and peptidyl-tRNA hydrolysis functions of Escherichia coli release factor 2 are linked through residue 246. RNA 6: 1704-1713.
    • (2000) RNA , vol.6 , pp. 1704-1713
    • Wilson, D.N.1    Guevremont, D.2    Tate, W.P.3
  • 41
    • 77952729843 scopus 로고    scopus 로고
    • Bioinformatic, structural, and functional analyses support release factor-like MTRF1 as a protein able to decode nonstandard stop codons beginning with adenine in vertebrate mitochondria
    • Young DJ, Edgar CD, Murphy J, Fredebohm J, Poole ES, Tate WP. 2010. Bioinformatic, structural, and functional analyses support release factor-like MTRF1 as a protein able to decode nonstandard stop codons beginning with adenine in vertebrate mitochondria. RNA 16: 1146-1155.
    • (2010) RNA , vol.16 , pp. 1146-1155
    • Young, D.J.1    Edgar, C.D.2    Murphy, J.3    Fredebohm, J.4    Poole, E.S.5    Tate, W.P.6
  • 42
    • 53849146066 scopus 로고    scopus 로고
    • Peptide release on the ribosome: Mechanism and implications for translational control
    • Youngman EM, McDonald ME, Green R. 2008. Peptide release on the ribosome: Mechanism and implications for translational control. Annu Rev Microbiol 62: 353-373.
    • (2008) Annu Rev Microbiol , vol.62 , pp. 353-373
    • Youngman, E.M.1    McDonald, M.E.2    Green, R.3
  • 43
    • 34047120718 scopus 로고    scopus 로고
    • Release factors 2 from Escherichia coli and Thermus thermophilus: Structural, spectroscopic and microcalorimetric studies
    • DOI 10.1093/nar/gkl696
    • Zoldak G, Redecke L, Svergun DI, Konarev PV, Voertler CS, Dobbek H, Sedlak E, Sprinzl M. 2007. Release factors 2 from Escherichia coli and Thermus thermophilus: Structural, spectroscopic and microcalorimetric studies. Nucleic Acids Res 35: 1343-1353. (Pubitemid 46522984)
    • (2007) Nucleic Acids Research , vol.35 , Issue.4 , pp. 1343-1353
    • Zoldak, G.1    Redecke, L.2    Svergun, D.I.3    Konarev, P.V.4    Voertler, C.S.5    Dobbek, H.6    Sedlak, E.7    Sprinzl, M.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.