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Volumn 21, Issue 7, 2013, Pages 1258-1263

Crystal structure of the 70S ribosome bound with the Q253P mutant form of release factor RF2

Author keywords

[No Author keywords available]

Indexed keywords

AMIDE; BACTERIAL PROTEIN; GLUTAMINE; MUTANT PROTEIN; NUCLEOTIDE; PROLINE; RELEASE FACTOR 2; TRANSFER RNA; UNCLASSIFIED DRUG;

EID: 84879837060     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2013.04.028     Document Type: Article
Times cited : (28)

References (50)
  • 2
    • 47949094068 scopus 로고    scopus 로고
    • Peptide release on the ribosome depends critically on the 2′ OH of the peptidyl-tRNA substrate
    • J.L. Brunelle, J.J. Shaw, E.M. Youngman, and R. Green Peptide release on the ribosome depends critically on the 2′ OH of the peptidyl-tRNA substrate RNA 14 2008 1526 1531
    • (2008) RNA , vol.14 , pp. 1526-1531
    • Brunelle, J.L.1    Shaw, J.J.2    Youngman, E.M.3    Green, R.4
  • 4
    • 0014126461 scopus 로고
    • Polypeptide chain termination in vitro: Isolation of a release factor
    • M.R. Capecchi Polypeptide chain termination in vitro: isolation of a release factor Proc. Natl. Acad. Sci. USA 58 1967 1144 1151
    • (1967) Proc. Natl. Acad. Sci. USA , vol.58 , pp. 1144-1151
    • Capecchi, M.R.1
  • 5
    • 0014631155 scopus 로고
    • Characterization of three proteins involved in polypeptide chain termination
    • M.R. Capecchi, and H.A. Klein Characterization of three proteins involved in polypeptide chain termination Cold Spring Harb. Symp. Quant. Biol. 34 1969 469 477
    • (1969) Cold Spring Harb. Symp. Quant. Biol. , vol.34 , pp. 469-477
    • Capecchi, M.R.1    Klein, H.A.2
  • 9
    • 77952928661 scopus 로고    scopus 로고
    • Ribosome structure and dynamics during translocation and termination
    • J.A. Dunkle, and J.H. Cate Ribosome structure and dynamics during translocation and termination Annu. Rev. Biophys. 39 2010 227 244
    • (2010) Annu. Rev. Biophys. , vol.39 , pp. 227-244
    • Dunkle, J.A.1    Cate, J.H.2
  • 11
    • 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
    • L.Y. Frolova, R.Y. Tsivkovskii, G.F. Sivolobova, N.Y. Oparina, O.I. Serpinsky, V.M. Blinov, S.I. Tatkov, and L.L. Kisselev 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 1999 1014 1020
    • (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
  • 12
    • 0037084101 scopus 로고    scopus 로고
    • The hemK gene in Escherichia coli encodes the N(5)-glutamine methyltransferase that modifies peptide release factors
    • V. Heurgué-Hamard, S. Champ, A. Engström, M. Ehrenberg, and R.H. Buckingham The hemK gene in Escherichia coli encodes the N(5)-glutamine methyltransferase that modifies peptide release factors EMBO J. 21 2002 769 778
    • (2002) EMBO J. , vol.21 , pp. 769-778
    • Heurgué-Hamard, V.1    Champ, S.2    Engström, A.3    Ehrenberg, M.4    Buckingham, R.H.5
  • 13
    • 13244259475 scopus 로고    scopus 로고
    • The glutamine residue of the conserved GGQ motif in Saccharomyces cerevisiae release factor eRF1 is methylated by the product of the YDR140w gene
    • V. Heurgué-Hamard, S. Champ, L. Mora, T. Merkulova-Rainon, L.L. Kisselev, and R.H. Buckingham The glutamine residue of the conserved GGQ motif in Saccharomyces cerevisiae release factor eRF1 is methylated by the product of the YDR140w gene J. Biol. Chem. 280 2005 2439 2445
    • (2005) J. Biol. Chem. , vol.280 , pp. 2439-2445
    • Heurgué-Hamard, V.1    Champ, S.2    Mora, L.3    Merkulova-Rainon, T.4    Kisselev, L.L.5    Buckingham, R.H.6
  • 15
    • 0034628438 scopus 로고    scopus 로고
    • A tripeptide 'anticodon' deciphers stop codons in messenger RNA
    • K. Ito, M. Uno, and Y. Nakamura A tripeptide 'anticodon' deciphers stop codons in messenger RNA Nature 403 2000 680 684
    • (2000) Nature , vol.403 , pp. 680-684
    • Ito, K.1    Uno, M.2    Nakamura, Y.3
  • 17
    • 0032717591 scopus 로고    scopus 로고
    • Bacterial biocatalysts: Molecular biology, three-dimensional structures, and biotechnological applications of lipases
    • K.E. Jaeger, B.W. Dijkstra, and M.T. Reetz Bacterial biocatalysts: molecular biology, three-dimensional structures, and biotechnological applications of lipases Annu. Rev. Microbiol. 53 1999 315 351
    • (1999) Annu. Rev. Microbiol. , vol.53 , pp. 315-351
    • Jaeger, K.E.1    Dijkstra, B.W.2    Reetz, M.T.3
  • 18
    • 77952685666 scopus 로고    scopus 로고
    • Structure of the 70S ribosome bound to release factor 2 and a substrate analog provides insights into catalysis of peptide release
    • H. Jin, A.C. Kelley, D. Loakes, and V. Ramakrishnan Structure of the 70S ribosome bound to release factor 2 and a substrate analog provides insights into catalysis of peptide release Proc. Natl. Acad. Sci. USA 107 2010 8593 8598
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 8593-8598
    • Jin, H.1    Kelley, A.C.2    Loakes, D.3    Ramakrishnan, V.4
  • 20
    • 84861425552 scopus 로고    scopus 로고
    • Linking crystallographic model and data quality
    • P.A. Karplus, and K. Diederichs Linking crystallographic model and data quality Science 336 2012 1030 1033
    • (2012) Science , vol.336 , pp. 1030-1033
    • Karplus, P.A.1    Diederichs, K.2
  • 22
    • 79955662779 scopus 로고    scopus 로고
    • Molecular recognition and catalysis in translation termination complexes
    • B.P. Klaholz Molecular recognition and catalysis in translation termination complexes Trends Biochem. Sci. 36 2011 282 292
    • (2011) Trends Biochem. Sci. , vol.36 , pp. 282-292
    • Klaholz, B.P.1
  • 23
    • 79960471842 scopus 로고    scopus 로고
    • Structural aspects of translation termination on the ribosome
    • A.A. Korostelev Structural aspects of translation termination on the ribosome RNA 17 2011 1409 1421
    • (2011) RNA , vol.17 , pp. 1409-1421
    • Korostelev, A.A.1
  • 25
    • 77955431163 scopus 로고    scopus 로고
    • Recognition of the amber UAG stop codon by release factor RF1
    • A. Korostelev, J. Zhu, H. Asahara, and H.F. Noller Recognition of the amber UAG stop codon by release factor RF1 EMBO J. 29 2010 2577 2585
    • (2010) EMBO J. , vol.29 , pp. 2577-2585
    • Korostelev, A.1    Zhu, J.2    Asahara, H.3    Noller, H.F.4
  • 26
    • 27944442879 scopus 로고    scopus 로고
    • Involvement of 16S rRNA nucleotides G1338 and A1339 in discrimination of initiator tRNA
    • L. Lancaster, and H.F. Noller Involvement of 16S rRNA nucleotides G1338 and A1339 in discrimination of initiator tRNA Mol. Cell 20 2005 623 632
    • (2005) Mol. Cell , vol.20 , pp. 623-632
    • Lancaster, L.1    Noller, H.F.2
  • 28
    • 77749322692 scopus 로고    scopus 로고
    • Structural and mechanistic insights into translation termination
    • P.G. Loh, and H. Song Structural and mechanistic insights into translation termination Curr. Opin. Struct. Biol. 20 2010 98 103
    • (2010) Curr. Opin. Struct. Biol. , vol.20 , pp. 98-103
    • Loh, P.G.1    Song, H.2
  • 29
    • 0037223622 scopus 로고    scopus 로고
    • The essential role of the invariant GGQ motif in the function and stability in vivo of bacterial release factors RF1 and RF2
    • L. Mora, V. Heurgué-Hamard, S. Champ, M. Ehrenberg, L.L. Kisselev, and R.H. Buckingham The essential role of the invariant GGQ motif in the function and stability in vivo of bacterial release factors RF1 and RF2 Mol. Microbiol. 47 2003 267 275
    • (2003) Mol. Microbiol. , vol.47 , pp. 267-275
    • Mora, L.1    Heurgué-Hamard, V.2    Champ, S.3    Ehrenberg, M.4    Kisselev, L.L.5    Buckingham, R.H.6
  • 30
    • 0037029037 scopus 로고    scopus 로고
    • A tripeptide discriminator for stop codon recognition
    • Y. Nakamura, and K. Ito A tripeptide discriminator for stop codon recognition FEBS Lett. 514 2002 30 33
    • (2002) FEBS Lett. , vol.514 , pp. 30-33
    • Nakamura, Y.1    Ito, K.2
  • 34
    • 33644818227 scopus 로고    scopus 로고
    • Interactions of the release factor RF1 with the ribosome as revealed by cryo-EM
    • U. Rawat, H. Gao, A. Zavialov, R. Gursky, M. Ehrenberg, and J. Frank Interactions of the release factor RF1 with the ribosome as revealed by cryo-EM J. Mol. Biol. 357 2006 1144 1153
    • (2006) J. Mol. Biol. , vol.357 , pp. 1144-1153
    • Rawat, U.1    Gao, H.2    Zavialov, A.3    Gursky, R.4    Ehrenberg, M.5    Frank, J.6
  • 35
    • 0014650139 scopus 로고
    • Peptide chain termination. V. The role of release factors in mRNA terminator codon recognition
    • E.M. Scolnick, and C.T. Caskey Peptide chain termination. V. The role of release factors in mRNA terminator codon recognition Proc. Natl. Acad. Sci. USA 64 1969 1235 1241
    • (1969) Proc. Natl. Acad. Sci. USA , vol.64 , pp. 1235-1241
    • Scolnick, E.M.1    Caskey, C.T.2
  • 37
    • 0034266465 scopus 로고    scopus 로고
    • Mutation of a glutamine residue in the universal tripeptide GGQ in human eRF1 termination factor does not cause complete loss of its activity
    • A. Seit-Nebi, L. Frolova, N. Ivanova, A. Poltaraus, and L. Kiselev [Mutation of a glutamine residue in the universal tripeptide GGQ in human eRF1 termination factor does not cause complete loss of its activity] Mol. Biol. (Mosk.) 34 2000 899 900
    • (2000) Mol. Biol. (Mosk.) , vol.34 , pp. 899-900
    • Seit-Nebi, A.1    Frolova, L.2    Ivanova, N.3    Poltaraus, A.4    Kiselev, L.5
  • 38
    • 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
    • A. Seit-Nebi, L. Frolova, J. Justesen, and L. Kisselev Class-1 translation termination factors: invariant GGQ minidomain is essential for release activity and ribosome binding but not for stop codon recognition Nucleic Acids Res. 29 2001 3982 3987
    • (2001) Nucleic Acids Res. , vol.29 , pp. 3982-3987
    • Seit-Nebi, A.1    Frolova, L.2    Justesen, J.3    Kisselev, L.4
  • 39
    • 35648950403 scopus 로고    scopus 로고
    • Two distinct components of release factor function uncovered by nucleophile partitioning analysis
    • J.J. Shaw, and R. Green Two distinct components of release factor function uncovered by nucleophile partitioning analysis Mol. Cell 28 2007 458 467
    • (2007) Mol. Cell , vol.28 , pp. 458-467
    • Shaw, J.J.1    Green, R.2
  • 40
    • 84865501655 scopus 로고    scopus 로고
    • A Role for the 2′ OH of peptidyl-tRNA substrate in peptide release on the ribosome revealed through RF-mediated rescue
    • J.J. Shaw, S. Trobro, S.L. He, J. Åqvist, and R. Green A Role for the 2′ OH of peptidyl-tRNA substrate in peptide release on the ribosome revealed through RF-mediated rescue Chem. Biol. 19 2012 983 993
    • (2012) Chem. Biol. , vol.19 , pp. 983-993
    • Shaw, J.J.1    Trobro, S.2    He, S.L.3    Åqvist, J.4    Green, R.5
  • 41
    • 0034603210 scopus 로고    scopus 로고
    • The crystal structure of human eukaryotic release factor eRF1 - Mechanism of stop codon recognition and peptidyl-tRNA hydrolysis
    • H. Song, P. Mugnier, A.K. Das, H.M. Webb, D.R. Evans, M.F. Tuite, B.A. Hemmings, and D. Barford The crystal structure of human eukaryotic release factor eRF1 - mechanism of stop codon recognition and peptidyl-tRNA hydrolysis Cell 100 2000 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
  • 42
    • 34548227759 scopus 로고    scopus 로고
    • A model for how ribosomal release factors induce peptidyl-tRNA cleavage in termination of protein synthesis
    • S. Trobro, and J. Aqvist A model for how ribosomal release factors induce peptidyl-tRNA cleavage in termination of protein synthesis Mol. Cell 27 2007 758 766
    • (2007) Mol. Cell , vol.27 , pp. 758-766
    • Trobro, S.1    Aqvist, J.2
  • 43
    • 72749108166 scopus 로고    scopus 로고
    • Mechanism of the translation termination reaction on the ribosome
    • S. Trobro, and J. Aqvist Mechanism of the translation termination reaction on the ribosome Biochemistry 48 2009 11296 11303
    • (2009) Biochemistry , vol.48 , pp. 11296-11303
    • Trobro, S.1    Aqvist, J.2
  • 44
    • 0014634150 scopus 로고
    • The possible involvement of peptidyl transferase in the termination step of protein biosynthesis
    • Z. Vogel, A. Zamir, and D. Elson The possible involvement of peptidyl transferase in the termination step of protein biosynthesis Biochemistry 8 1969 5161 5168
    • (1969) Biochemistry , vol.8 , pp. 5161-5168
    • Vogel, Z.1    Zamir, A.2    Elson, D.3
  • 45
    • 0035066836 scopus 로고    scopus 로고
    • Global indicators of X-ray data quality
    • M.S. Weiss Global indicators of X-ray data quality J. Appl. Crystallorg. 34 2001 130 135
    • (2001) J. Appl. Crystallorg. , vol.34 , pp. 130-135
    • Weiss, M.S.1
  • 48
    • 0036810254 scopus 로고    scopus 로고
    • Release of peptide promoted by the GGQ motif of class 1 release factors regulates the GTPase activity of RF3
    • A.V. Zavialov, L. Mora, R.H. Buckingham, and M. Ehrenberg Release of peptide promoted by the GGQ motif of class 1 release factors regulates the GTPase activity of RF3 Mol. Cell 10 2002 789 798
    • (2002) Mol. Cell , vol.10 , pp. 789-798
    • Zavialov, A.V.1    Mora, L.2    Buckingham, R.H.3    Ehrenberg, M.4
  • 49
    • 84870393666 scopus 로고    scopus 로고
    • Crystal structures of 70S ribosomes bound to release factors RF1, RF2 and RF3
    • J. Zhou, A. Korostelev, L. Lancaster, and H.F. Noller Crystal structures of 70S ribosomes bound to release factors RF1, RF2 and RF3 Curr. Opin. Struct. Biol. 22 2012 733 742
    • (2012) Curr. Opin. Struct. Biol. , vol.22 , pp. 733-742
    • Zhou, J.1    Korostelev, A.2    Lancaster, L.3    Noller, H.F.4
  • 50
    • 79952130828 scopus 로고    scopus 로고
    • Crystal structures of complexes containing domains from two viral internal ribosome entry site (IRES) RNAs bound to the 70S ribosome
    • J. Zhu, A. Korostelev, D.A. Costantino, J.P. Donohue, H.F. Noller, and J.S. Kieft Crystal structures of complexes containing domains from two viral internal ribosome entry site (IRES) RNAs bound to the 70S ribosome Proc. Natl. Acad. Sci. USA 108 2011 1839 1844
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 1839-1844
    • Zhu, J.1    Korostelev, A.2    Costantino, D.A.3    Donohue, J.P.4    Noller, H.F.5    Kieft, J.S.6


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