메뉴 건너뛰기




Volumn 43, Issue 18, 2015, Pages 8615-8626

Structure of a human translation termination complex

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN ERF1; TRANSLATION TERMINATION COMPLEX; TRANSLATION TERMINATION FACTOR; UNCLASSIFIED DRUG; ETF1 PROTEIN, HUMAN; PEPTIDE; STOP CODON;

EID: 84957605728     PISSN: 03051048     EISSN: 13624962     Source Type: Journal    
DOI: 10.1093/nar/gkv909     Document Type: Article
Times cited : (90)

References (58)
  • 1
    • 0038403669 scopus 로고    scopus 로고
    • Insights into the decoding mechanism from recent ribosome structures
    • Ogle, J.M., Carter, A.P. and Ramakrishnan, V. (2003) Insights into the decoding mechanism from recent ribosome structures. Trends Biochem. Sci., 28, 259-266.
    • (2003) Trends Biochem. Sci , vol.28 , pp. 259-266
    • Ogle, J.M.1    Carter, A.P.2    Ramakrishnan, V.3
  • 2
    • 84859593945 scopus 로고    scopus 로고
    • A new understanding of the decoding principle on the ribosome
    • Demeshkina, N., Jenner, L., Westhof, E., Yusupov, M. and Yusupova, G. (2012) A new understanding of the decoding principle on the ribosome. Nature, 484, 256-259.
    • (2012) Nature , vol.484 , pp. 256-259
    • Demeshkina, N.1    Jenner, L.2    Westhof, E.3    Yusupov, M.4    Yusupova, G.5
  • 3
    • 84870393666 scopus 로고    scopus 로고
    • Crystal structures of 70S ribosomes bound to release factors RF1, RF2 and RF3
    • Zhou, J., Korostelev, A., Lancaster, L. and Noller, H.F. (2012) Crystal structures of 70S ribosomes bound to release factors RF1, RF2 and RF3. Curr. Opin. Struct. Biol., 22, 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
  • 4
    • 79960471842 scopus 로고    scopus 로고
    • Structural aspects of translation termination on the ribosome
    • Korostelev, A.A. (2011) Structural aspects of translation termination on the ribosome. RNA, 17, 1409-1421.
    • (2011) RNA , vol.17 , pp. 1409-1421
    • Korostelev, A.A.1
  • 5
    • 84881113615 scopus 로고    scopus 로고
    • The ribosome as a versatile catalyst: Reactions at the peptidyl transferase center
    • Rodnina, M.V. (2013) The ribosome as a versatile catalyst: reactions at the peptidyl transferase center. Curr. Opin. Struct. Biol., 23, 595-602.
    • (2013) Curr. Opin. Struct. Biol , vol.23 , pp. 595-602
    • Rodnina, M.V.1
  • 8
    • 55849143658 scopus 로고    scopus 로고
    • Insights into translational termination from the structure of rf2 bound to the ribosome
    • Weixlbaumer, A., Jin, H., Neubauer, C., Voorhees, R.M., Petry, S., Kelley, A.C. and Ramakrishnan, V. (2008) Insights into Translational Termination from the Structure of RF2 Bound to the Ribosome. Science (80)., 322, 953-956.
    • (2008) Science , vol.80 , Issue.322 , pp. 953-956
    • Weixlbaumer, A.1    Jin, H.2    Neubauer, C.3    Voorhees, R.M.4    Petry, S.5    Kelley, A.C.6    Ramakrishnan, V.7
  • 9
    • 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
    • Jin, H., Kelley, A.C., Loakes, D. and Ramakrishnan, V. (2010) 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. U.S.A., 107, 8593-8598.
    • (2010) Proc. Natl. Acad. Sci. U.S.A , vol.107 , pp. 8593-8598
    • Jin, H.1    Kelley, A.C.2    Loakes, D.3    Ramakrishnan, V.4
  • 10
    • 0033827056 scopus 로고    scopus 로고
    • Terminating eukaryote translation: Domain 1 of release factor eRF1 functions in stop codon recognition
    • Bertram, G., Bell, H.A., Ritchie, D.W., Fullerton, G. and Stansfield, I. (2000) Terminating eukaryote translation: domain 1 of release factor eRF1 functions in stop codon recognition. RNA, 6, 1236-1247.
    • (2000) RNA , vol.6 , pp. 1236-1247
    • Bertram, G.1    Bell, H.A.2    Ritchie, D.W.3    Fullerton, G.4    Stansfield, I.5
  • 11
    • 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. and 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
  • 15
    • 84855501083 scopus 로고    scopus 로고
    • Kinetic analysis reveals the ordered coupling of translation termination and ribosome recycling in yeast
    • Shoemaker, C.J. and Green, R. (2011) Kinetic analysis reveals the ordered coupling of translation termination and ribosome recycling in yeast. Proc. Natl. Acad. Sci. U.S.A., 108, E1392-E1398.
    • (2011) Proc. Natl. Acad. Sci. U.S.A , vol.108 , pp. E1392-E1398
    • Shoemaker, C.J.1    Green, R.2
  • 16
    • 33744993160 scopus 로고    scopus 로고
    • In vitro reconstitution of eukaryotic translation reveals cooperativity between release factors eRF1 and eRF3
    • Alkalaeva, E.Z., Pisarev, A.V., Frolova, L.Y., Kisselev, L.L. and Pestova, T.V. (2006) In vitro reconstitution of eukaryotic translation reveals cooperativity between release factors eRF1 and eRF3. Cell, 125, 1125-1136.
    • (2006) Cell , vol.125 , pp. 1125-1136
    • Alkalaeva, E.Z.1    Pisarev, A.V.2    Frolova, L.Y.3    Kisselev, L.L.4    Pestova, T.V.5
  • 17
    • 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. and 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
  • 18
    • 84924918778 scopus 로고    scopus 로고
    • Cryo-EM of ribosomal 80S complexes with termination factors reveals the translocated cricket paralysis virus IRES
    • Muhs, M., Hilal, T., Mielke, T., Skabkin, M.A., Sanbonmatsu, K.Y., Pestova, T.V. and Spahn, C.M.T. (2015) Cryo-EM of ribosomal 80S complexes with termination factors reveals the translocated cricket paralysis virus IRES. Mol. Cell, 57, 422-432.
    • (2015) Mol. Cell , vol.57 , pp. 422-432
    • Muhs, M.1    Hilal, T.2    Mielke, T.3    Skabkin, M.A.4    Sanbonmatsu, K.Y.5    Pestova, T.V.6    Spahn, C.M.T.7
  • 20
    • 79952750280 scopus 로고    scopus 로고
    • Ribosome recycling depends on a mechanistic link between the FeS cluster domain and a conformational switch of the twin-ATPase ABCE1
    • Barthelme, D., Dinkelaker, S., Albers, S.-V., Londei, P., Ermler, U. and Tampé, R. (2011) Ribosome recycling depends on a mechanistic link between the FeS cluster domain and a conformational switch of the twin-ATPase ABCE1. Proc. Natl. Acad. Sci. U.S.A., 108, 3228-3233.
    • (2011) Proc. Natl. Acad. Sci. U.S.A , vol.108 , pp. 3228-3233
    • Barthelme, D.1    Dinkelaker, S.2    Albers, S.-V.3    Londei, P.4    Ermler, U.5    Tampé, R.6
  • 23
    • 0036216442 scopus 로고    scopus 로고
    • Highly conserved NIKS tetrapeptide is functionally essential in eukaryotic translation termination factor eRF1
    • Frolova, L., Seit-Nebi, A. and 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
  • 24
    • 84863226738 scopus 로고    scopus 로고
    • Selectivity of stop codon recognition in translation termination is modulated by multiple conformations of GTS loop in eRF1
    • Wong, L.E., Li, Y., Pillay, S., Frolova, L. and Pervushin, K. (2012) Selectivity of stop codon recognition in translation termination is modulated by multiple conformations of GTS loop in eRF1. Nucleic Acids Res., 40, 5751-5765.
    • (2012) Nucleic Acids Res , vol.40 , pp. 5751-5765
    • Wong, L.E.1    Li, Y.2    Pillay, S.3    Frolova, L.4    Pervushin, K.5
  • 25
    • 84861385710 scopus 로고    scopus 로고
    • Identification of eRF1 residues that play critical and complementary roles in stop codon recognition
    • Conard, S.E., Buckley, J., Dang, M., Bedwell, G.J., Carter, R.L., Khass, M. and Bedwell, D.M. (2012) Identification of eRF1 residues that play critical and complementary roles in stop codon recognition. RNA, 18, 1210-1221.
    • (2012) RNA , vol.18 , pp. 1210-1221
    • Conard, S.E.1    Buckley, J.2    Dang, M.3    Bedwell, G.J.4    Carter, R.L.5    Khass, M.6    Bedwell, D.M.7
  • 26
    • 0036747332 scopus 로고    scopus 로고
    • Conversion of omnipotent translation termination factor eRF1 into ciliate-like UGA-only unipotent eRF1
    • Seit-Nebi, A. (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
  • 27
    • 79957465901 scopus 로고    scopus 로고
    • MEGAWHOP cloning: A method of creating random mutagenesis libraries via megaprimer PCR of whole plasmids
    • Miyazaki, K. (2011) MEGAWHOP cloning: a method of creating random mutagenesis libraries via megaprimer PCR of whole plasmids. Methods Enzymol, 498, 399-406.
    • (2011) Methods Enzymol , vol.498 , pp. 399-406
    • Miyazaki, K.1
  • 29
    • 77952760591 scopus 로고    scopus 로고
    • Cell-free protein synthesis systems with extracts from cultured human cells
    • Mikami, S., Kobayashi, T. and Imataka, H. (2010) Cell-free protein synthesis systems with extracts from cultured human cells. Methods Mol. Biol., 607, 43-52.
    • (2010) Methods Mol. Biol , vol.607 , pp. 43-52
    • Mikami, S.1    Kobayashi, T.2    Imataka, H.3
  • 30
    • 0035798359 scopus 로고    scopus 로고
    • Architecture of the protein-conducting channel associated with the translating 80S ribosome
    • Beckmann, R., Spahn, C.M., Eswar, N., Helmers, J., Penczek, P.A., Sali, A., Frank, J. and Blobel, G. (2001) Architecture of the protein-conducting channel associated with the translating 80S ribosome. Cell, 107, 361-372.
    • (2001) Cell , vol.107 , pp. 361-372
    • Beckmann, R.1    Spahn, C.M.2    Eswar, N.3    Helmers, J.4    Penczek, P.A.5    Sali, A.6    Frank, J.7    Blobel, G.8
  • 31
    • 1542319100 scopus 로고    scopus 로고
    • Structure of the signal recognition particle interacting with the elongation-arrested ribosome
    • Halic, M., Becker, T., Pool, M.R., Spahn, C.M., Grassucci, R.A., Frank, J. and Beckmann, R. (2004) Structure of the signal recognition particle interacting with the elongation-arrested ribosome. Nature, 427, 808-814.
    • (2004) Nature , vol.427 , pp. 808-814
    • Halic, M.1    Becker, T.2    Pool, M.R.3    Spahn, C.M.4    Grassucci, R.A.5    Frank, J.6    Beckmann, R.7
  • 32
    • 84880848354 scopus 로고    scopus 로고
    • Electron counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM
    • Li, X., Mooney, P., Zheng, S., Booth, C.R., Braunfeld, M.B., Gubbens, S., Agard, D.A. and Cheng, Y. (2013) Electron counting and beam-induced motion correction enable near-atomic-resolution single-particle cryo-EM. Nat. Methods, 10, 584-590.
    • (2013) Nat. Methods , vol.10 , pp. 584-590
    • Li, X.1    Mooney, P.2    Zheng, S.3    Booth, C.R.4    Braunfeld, M.B.5    Gubbens, S.6    Agard, D.A.7    Cheng, Y.8
  • 33
    • 33845449481 scopus 로고    scopus 로고
    • SIGNATURE: A single-particle selection system for molecular electron microscopy
    • Chen, J.Z. and Grigorieff, N. (2007) SIGNATURE: a single-particle selection system for molecular electron microscopy. J. Struct. Biol., 157, 168-173.
    • (2007) J. Struct. Biol , vol.157 , pp. 168-173
    • Chen, J.Z.1    Grigorieff, N.2
  • 34
    • 0029975088 scopus 로고    scopus 로고
    • SPIDER and WEB: Processing and visualization of images in 3D electron microscopy and related fields
    • Frank, J., Radermacher, M., Penczek, P., Zhu, J., Li, Y., Ladjadj, M. and Leith, A. (1996) SPIDER and WEB: processing and visualization of images in 3D electron microscopy and related fields. J. Struct. Biol., 116, 190-199.
    • (1996) J. Struct. Biol , vol.116 , pp. 190-199
    • Frank, J.1    Radermacher, M.2    Penczek, P.3    Zhu, J.4    Li, Y.5    Ladjadj, M.6    Leith, A.7
  • 36
    • 84894623755 scopus 로고    scopus 로고
    • Quantifying the local resolution of cryo-EM density maps
    • Kucukelbir, A., Sigworth, F.J. and Tagare, H.D. (2014) Quantifying the local resolution of cryo-EM density maps. Nat. Methods, 11, 63-65.
    • (2014) Nat. Methods , vol.11 , pp. 63-65
    • Kucukelbir, A.1    Sigworth, F.J.2    Tagare, H.D.3
  • 37
    • 84866078359 scopus 로고    scopus 로고
    • Prevention of overfitting in cryo-EM structure determination
    • Scheres, S.H.W. and Chen, S. (2012) Prevention of overfitting in cryo-EM structure determination. Nat. Methods, 9, 853-854.
    • (2012) Nat. Methods , vol.9 , pp. 853-854
    • Scheres, S.H.W.1    Chen, S.2
  • 38
    • 51549084591 scopus 로고    scopus 로고
    • Sharpening high resolution information in single particle electron cryomicroscopy
    • Fernández, J.J., Luque, D., Castón, J.R. and Carrascosa, J.L. (2008) Sharpening high resolution information in single particle electron cryomicroscopy. J. Struct. Biol., 164, 170-175.
    • (2008) J. Struct. Biol , vol.164 , pp. 170-175
    • Fernández, J.J.1    Luque, D.2    Castón, J.R.3    Carrascosa, J.L.4
  • 43
    • 0027234622 scopus 로고
    • Translational inhibition mediated by a short upstream open reading frame in the human cytomegalovirus gpUL4 (gp48) transcript
    • Degnin, C.R., Schleiss, M.R., Cao, J. and Geballe, A.P. (1993) Translational inhibition mediated by a short upstream open reading frame in the human cytomegalovirus gpUL4 (gp48) transcript. J. Virol., 67, 5514-5521.
    • (1993) J. Virol , vol.67 , pp. 5514-5521
    • Degnin, C.R.1    Schleiss, M.R.2    Cao, J.3    Geballe, A.P.4
  • 44
    • 0036893271 scopus 로고    scopus 로고
    • Inhibition of translation termination mediated by an interaction of eukaryotic release factor 1 with a nascent peptidyl-tRNA
    • Janzen, D.M., Frolova, L. and Geballe, A.P. (2002) Inhibition of translation termination mediated by an interaction of eukaryotic release factor 1 with a nascent peptidyl-tRNA. Mol. Cell. Biol., 22, 8562-8570.
    • (2002) Mol. Cell. Biol , vol.22 , pp. 8562-8570
    • Janzen, D.M.1    Frolova, L.2    Geballe, A.P.3
  • 45
    • 0034682720 scopus 로고    scopus 로고
    • Initiation of protein synthesis from the A site of the ribosome
    • Wilson, J.E., Pestova, T. V, Hellen, C.U. and Sarnow, P. (2000) Initiation of protein synthesis from the A site of the ribosome. Cell, 102, 511-520.
    • (2000) Cell , vol.102 , pp. 511-520
    • Wilson, J.E.1    Pestova, T.V.2    Hellen, C.U.3    Sarnow, P.4
  • 49
    • 2542470615 scopus 로고    scopus 로고
    • The active site of the ribosome is composed of two layers of conserved nucleotides with distinct roles in peptide bond formation and peptide release
    • Youngman, E.M., Brunelle, J.L., Kochaniak, A.B. and Green, R. (2004) The active site of the ribosome is composed of two layers of conserved nucleotides with distinct roles in peptide bond formation and peptide release. Cell, 117, 589-599.
    • (2004) Cell , vol.117 , pp. 589-599
    • Youngman, E.M.1    Brunelle, J.L.2    Kochaniak, A.B.3    Green, R.4
  • 51
    • 0034697987 scopus 로고    scopus 로고
    • Predicting U-turns in ribosomal RNA with comparative sequence analysis
    • Gutell, R.R., Cannone, J.J., Konings, D. and Gautheret, D. (2000) Predicting U-turns in ribosomal RNA with comparative sequence analysis. J. Mol. Biol., 300, 791-803.
    • (2000) J. Mol. Biol , vol.300 , pp. 791-803
    • Gutell, R.R.1    Cannone, J.J.2    Konings, D.3    Gautheret, D.4
  • 53
    • 84936806750 scopus 로고    scopus 로고
    • Genetic analysis of L123 of the tRNA-mimicking eukaryote release factor eRF1, an amino acid residue critical for discrimination of stop codons
    • Saito, K. and Ito, K. (2015) Genetic analysis of L123 of the tRNA-mimicking eukaryote release factor eRF1, an amino acid residue critical for discrimination of stop codons. Nucleic Acids Res., 43, 4591-4601.
    • (2015) Nucleic Acids Res , vol.43 , pp. 4591-4601
    • Saito, K.1    Ito, K.2
  • 54
    • 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. and Favre, A. (2002) The invariant uridine of stop codons contacts the conserved NIKSR loop of human eRF1 in the ribosome. EMBO J., 21, 5302-5311.
    • (2002) EMBO J , vol.21 , pp. 5302-5311
    • Chavatte, L.1    Seit-Nebi, A.2    Dubovaya, V.3    Favre, A.4
  • 55
    • 0029118487 scopus 로고
    • A free energy analysis of nucleic acid base stacking in aqueous solution
    • Friedman, R.A. and Honig, B. (1995) A free energy analysis of nucleic acid base stacking in aqueous solution. Biophys. J., 69, 1528-1535.
    • (1995) Biophys. J , vol.69 , pp. 1528-1535
    • Friedman, R.A.1    Honig, B.2
  • 56
    • 84861385710 scopus 로고    scopus 로고
    • Identification of eRF1 residues that play critical and complementary roles in stop codon recognition
    • Conard, S.E., Buckley, J., Dang, M., Bedwell, G.J., Carter, R.L., Khass, M. and Bedwell, D.M. (2012) Identification of eRF1 residues that play critical and complementary roles in stop codon recognition. RNA, 18, 1210-1221.
    • (2012) RNA , vol.18 , pp. 1210-1221
    • Conard, S.E.1    Buckley, J.2    Dang, M.3    Bedwell, G.J.4    Carter, R.L.5    Khass, M.6    Bedwell, D.M.7
  • 58
    • 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.