메뉴 건너뛰기




Volumn 15, Issue 3 SPEC. ISS., 2005, Pages 349-354

Elongation factors on the ribosome

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; ELONGATION FACTOR; ELONGATION FACTOR G; ELONGATION FACTOR TU; GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATASE; GUANOSINE TRIPHOSPHATE; MESSENGER RNA; TRANSFER RNA;

EID: 20444490272     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.sbi.2005.05.004     Document Type: Review
Times cited : (76)

References (33)
  • 1
  • 4
    • 0014690239 scopus 로고
    • Studies on the formation of transfer ribonucleic acid-ribosome complexes. VI. Oligopeptide synthesis and translocation on ribosomes in the presence and absence of soluble transfer factors
    • S. Pestka Studies on the formation of transfer ribonucleic acid-ribosome complexes. VI. Oligopeptide synthesis and translocation on ribosomes in the presence and absence of soluble transfer factors J Biol Chem 244 1969 1533 1539
    • (1969) J Biol Chem , vol.244 , pp. 1533-1539
    • Pestka, S.1
  • 5
    • 0042173407 scopus 로고    scopus 로고
    • Ribosomal proteins S12 and S13 function as control elements for translocation of the mRNA:tRNA complex
    • A.R. Cukras, D.R. Southworth, J.L. Brunelle, G.M. Culver, and R. Green Ribosomal proteins S12 and S13 function as control elements for translocation of the mRNA:tRNA complex Mol Cell 12 2003 321 328
    • (2003) Mol Cell , vol.12 , pp. 321-328
    • Cukras, A.R.1    Southworth, D.R.2    Brunelle, J.L.3    Culver, G.M.4    Green, R.5
  • 6
    • 0031028688 scopus 로고    scopus 로고
    • Hydrolysis of GTP by elongation factor G drives tRNA movement on the ribosome
    • M.V. Rodnina, A. Savelsbergh, V.I. Katunin, and W. Wintermeyer Hydrolysis of GTP by elongation factor G drives tRNA movement on the ribosome Nature 385 1997 37 41
    • (1997) Nature , vol.385 , pp. 37-41
    • Rodnina, M.V.1    Savelsbergh, A.2    Katunin, V.I.3    Wintermeyer, W.4
  • 8
    • 0038403669 scopus 로고    scopus 로고
    • Insights into the decoding mechanism from recent ribosome structures
    • J.M. Ogle, A.P. Carter, and V. Ramakrishnan Insights into the decoding mechanism from recent ribosome structures Trends Biochem Sci 28 2003 259 266
    • (2003) Trends Biochem Sci , vol.28 , pp. 259-266
    • Ogle, J.M.1    Carter, A.P.2    Ramakrishnan, V.3
  • 9
    • 0842267211 scopus 로고    scopus 로고
    • Kinetic determinants of high-fidelity tRNA discrimination on the ribosome
    • K.B. Gromadski, and M.V. Rodnina Kinetic determinants of high-fidelity tRNA discrimination on the ribosome Mol Cell 13 2004 191 200
    • (2004) Mol Cell , vol.13 , pp. 191-200
    • Gromadski, K.B.1    Rodnina, M.V.2
  • 10
    • 0033168212 scopus 로고    scopus 로고
    • Induced fit in initial selection and proofreading of aminoacyl-tRNA on the ribosome
    • T. Pape, W. Wintermeyer, and M. Rodnina Induced fit in initial selection and proofreading of aminoacyl-tRNA on the ribosome EMBO J 18 1999 3800 3807
    • (1999) EMBO J , vol.18 , pp. 3800-3807
    • Pape, T.1    Wintermeyer, W.2    Rodnina, M.3
  • 11
    • 4744365694 scopus 로고    scopus 로고
    • TRNA selection and kinetic proofreading in translation
    • S.C. Blanchard, R.L. Gonzalez, H.D. Kim, S. Chu, and J.D. Puglisi tRNA selection and kinetic proofreading in translation Nat Struct Mol Biol 11 2004 1008 1014 Using single-molecule fluorescence techniques, the delivery and selection of aa-tRNA was studied. The authors identify novel tRNA states on the ribosome and the method reveals the dynamics of the process.
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 1008-1014
    • Blanchard, S.C.1    Gonzalez, R.L.2    Kim, H.D.3    Chu, S.4    Puglisi, J.D.5
  • 12
    • 0037184536 scopus 로고    scopus 로고
    • Selection of tRNA by the ribosome requires a transition from an open to a closed form
    • J.M. Ogle, F.V. Murphy, M.J. Tarry, and V. Ramakrishnan Selection of tRNA by the ribosome requires a transition from an open to a closed form Cell 111 2002 721 732
    • (2002) Cell , vol.111 , pp. 721-732
    • Ogle, J.M.1    Murphy, F.V.2    Tarry, M.J.3    Ramakrishnan, V.4
  • 13
    • 1842420639 scopus 로고    scopus 로고
    • Streptomycin interferes with conformational coupling between codon recognition and GTPase activation on the ribosome
    • K.B. Gromadski, and M.V. Rodnina Streptomycin interferes with conformational coupling between codon recognition and GTPase activation on the ribosome Nat Struct Mol Biol 11 2004 316 322
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 316-322
    • Gromadski, K.B.1    Rodnina, M.V.2
  • 14
    • 0242407184 scopus 로고    scopus 로고
    • Incorporation of aminoacyl-tRNA into the ribosome as seen by cryo-electron microscopy
    • M. Valle, A. Zavialov, W. Li, S.M. Stagg, J. Sengupta, R.C. Nielsen, P. Nissen, S.C. Harvey, M. Ehrenberg, and J. Frank Incorporation of aminoacyl-tRNA into the ribosome as seen by cryo-electron microscopy Nat Struct Biol 10 2003 899 906 A 9 Å cryo-EM map of the ternary complex on the ribosome is presented. The map shows a kink in the tRNA structure during the delivery process, and shines light on the coupling between decoding and stimulation of the GTPase activity of EF-Tu.
    • (2003) Nat Struct Biol , vol.10 , pp. 899-906
    • Valle, M.1    Zavialov, A.2    Li, W.3    Stagg, S.M.4    Sengupta, J.5    Nielsen, R.C.6    Nissen, P.7    Harvey, S.C.8    Ehrenberg, M.9    Frank, J.10
  • 16
    • 0024458904 scopus 로고
    • Intermediate states in the movement of transfer RNA in the ribosome
    • D. Moazed, and H.F. Noller Intermediate states in the movement of transfer RNA in the ribosome Nature 342 1989 142 148
    • (1989) Nature , vol.342 , pp. 142-148
    • Moazed, D.1    Noller, H.F.2
  • 17
    • 0035942248 scopus 로고    scopus 로고
    • RNA tertiary interactions in the large ribosomal subunit: The A-minor motif
    • P. Nissen, J. Ippolito, N. Ban, P.B. Moore, and T.A. Steitz RNA tertiary interactions in the large ribosomal subunit: the A-minor motif Proc Natl Acad Sci USA 98 2001 4899 4903
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 4899-4903
    • Nissen, P.1    Ippolito, J.2    Ban, N.3    Moore, P.B.4    Steitz, T.A.5
  • 18
    • 0037015077 scopus 로고    scopus 로고
    • Specificity of RNA-RNA helix recognition
    • D.J. Battle, and J. Doudna Specificity of RNA-RNA helix recognition Proc Natl Acad Sci USA 99 2002 11676 11681
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 11676-11681
    • Battle, D.J.1    Doudna, J.2
  • 19
    • 0033762347 scopus 로고    scopus 로고
    • Energetic contribution of tRNA hybrid state formation to translocation catalysis on the ribosome
    • Y.P. Semenkov, M.V. Rodnina, and W. Wintermeyer Energetic contribution of tRNA hybrid state formation to translocation catalysis on the ribosome Nat Struct Biol 7 2000 1027 1031
    • (2000) Nat Struct Biol , vol.7 , pp. 1027-1031
    • Semenkov, Y.P.1    Rodnina, M.V.2    Wintermeyer, W.3
  • 20
    • 4444313551 scopus 로고    scopus 로고
    • TRNA dynamics on the ribosome during translation
    • S.C. Blanchard, H.D. Kim, R.L. Gonzalez Jr., J.D. Puglisi, and S. Chu tRNA dynamics on the ribosome during translation Proc Natl Acad Sci USA 101 2004 12893 12898 A system for studying translation on single ribosomes is presented. It reveals that tRNAs rapidly equilibrate between classical and hybrid states on the ribosome.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 12893-12898
    • Blanchard, S.C.1    Kim, H.D.2    Gonzalez Jr., R.L.3    Puglisi, J.D.4    Chu, S.5
  • 21
    • 0037963475 scopus 로고    scopus 로고
    • Locking and unlocking of ribosomal motions
    • M. Valle, A. Zavialov, J. Sengupta, U. Rawat, M. Ehrenberg, and J. Frank Locking and unlocking of ribosomal motions Cell 114 2003 123 134 Several complexes of EF-G bound to the ribosome are visualized by cryo-EM. The study reveals that only when a peptidyl-tRNA is absent from the P-site will EF-G induce the ratchet motion of the two subunits.
    • (2003) Cell , vol.114 , pp. 123-134
    • Valle, M.1    Zavialov, A.2    Sengupta, J.3    Rawat, U.4    Ehrenberg, M.5    Frank, J.6
  • 24
    • 0038286524 scopus 로고    scopus 로고
    • Catalysis of ribosomal translocation by sparsomycin
    • K. Fredrick, and H.F. Noller Catalysis of ribosomal translocation by sparsomycin Science 300 2003 1159 1162 It is shown that the compound sparsomycin can catalyze accurate translocation of tRNA, supporting the notion that translocation is an inherent activity of the ribosome.
    • (2003) Science , vol.300 , pp. 1159-1162
    • Fredrick, K.1    Noller, H.F.2
  • 25
    • 0038300651 scopus 로고    scopus 로고
    • Peptidyl-tRNA regulates the GTPase activity of translation factors
    • A.V. Zavialov, and M. Ehrenberg Peptidyl-tRNA regulates the GTPase activity of translation factors Cell 114 2003 113 122 An efficient in vitro system with well-defined ribosome complexes shows that the peptidyl-tRNA in the P-site regulates the activity of EF-G, but not that of the ternary complex. The study explains how the activities of the elongation factors are coordinated.
    • (2003) Cell , vol.114 , pp. 113-122
    • Zavialov, A.V.1    Ehrenberg, M.2
  • 26
    • 0034637111 scopus 로고    scopus 로고
    • The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution
    • N. Ban, P. Nissen, J. Hansen, P.B. Moore, and T.A. Steitz The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution Science 289 2000 905 920
    • (2000) Science , vol.289 , pp. 905-920
    • Ban, N.1    Nissen, P.2    Hansen, J.3    Moore, P.B.4    Steitz, T.A.5
  • 27
    • 0038433302 scopus 로고    scopus 로고
    • An elongation factor G-induced ribosome rearrangement precedes tRNA-mRNA translocation
    • A. Savelsbergh, V.I. Katunin, D. Mohr, F. Peske, M.V. Rodnina, and W. Wintermeyer An elongation factor G-induced ribosome rearrangement precedes tRNA-mRNA translocation Mol Cell 11 2003 1517 1523 A thorough kinetic analysis of the translocation process is presented. The study reveals that the rate-limiting step of translocation is a rearrangement of the ribosome driven by GTP hydrolysis on EF-G.
    • (2003) Mol Cell , vol.11 , pp. 1517-1523
    • Savelsbergh, A.1    Katunin, V.I.2    Mohr, D.3    Peske, F.4    Rodnina, M.V.5    Wintermeyer, W.6
  • 28
    • 0034691576 scopus 로고    scopus 로고
    • A ratchet-like inter-subunit reorganization of the ribosome during translocation
    • J. Frank, and R.K. Agrawal A ratchet-like inter-subunit reorganization of the ribosome during translocation Nature 406 2000 318 322
    • (2000) Nature , vol.406 , pp. 318-322
    • Frank, J.1    Agrawal, R.K.2
  • 29
    • 0032982866 scopus 로고    scopus 로고
    • EF-G-dependent GTP hydrolysis induces translocation accompanied by large conformational changes in the 70S ribosome
    • R.K. Agrawal, A.B. Heagle, P. Penczek, R.A. Grassucci, and J. Frank EF-G-dependent GTP hydrolysis induces translocation accompanied by large conformational changes in the 70S ribosome Nat Struct Biol 6 1999 643 647
    • (1999) Nat Struct Biol , vol.6 , pp. 643-647
    • Agrawal, R.K.1    Heagle, A.B.2    Penczek, P.3    Grassucci, R.A.4    Frank, J.5
  • 30
    • 0033638447 scopus 로고    scopus 로고
    • Conformationally restricted elongation factor G retains GTPase activity but is inactive in translocation on the ribosome
    • F. Peske, N.B. Matassova, A. Savelsbergh, M.V. Rodnina, and W. Wintermeyer Conformationally restricted elongation factor G retains GTPase activity but is inactive in translocation on the ribosome Mol Cell 6 2000 501 505
    • (2000) Mol Cell , vol.6 , pp. 501-505
    • Peske, F.1    Matassova, N.B.2    Savelsbergh, A.3    Rodnina, M.V.4    Wintermeyer, W.5
  • 31
    • 0242516080 scopus 로고    scopus 로고
    • Two crystal structures demonstrate large conformational changes in the eukaryotic ribosomal translocase
    • R. Jorgensen, P.A. Ortiz, A. Carr-Schmid, P. Nissen, T.G. Kinzy, and G.R. Andersen Two crystal structures demonstrate large conformational changes in the eukaryotic ribosomal translocase Nat Struct Biol 10 2003 379 385 Crystal structures of the eukaryotic translocase, eEF2, solved with and without sordarin reveal large conformational changes.
    • (2003) Nat Struct Biol , vol.10 , pp. 379-385
    • Jorgensen, R.1    Ortiz, P.A.2    Carr-Schmid, A.3    Nissen, P.4    Kinzy, T.G.5    Andersen, G.R.6
  • 33
    • 0030850032 scopus 로고    scopus 로고
    • The conformational properties of elongation factor G and the mechanism of translocation
    • J. Czworkowski, and P.B. Moore The conformational properties of elongation factor G and the mechanism of translocation Biochemistry 36 1997 10327 10334
    • (1997) Biochemistry , vol.36 , pp. 10327-10334
    • Czworkowski, J.1    Moore, P.B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.