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Volumn 29, Issue 4, 2010, Pages 770-781

A fast dynamic mode of the EF-G-bound ribosome

Author keywords

EF G; Ribosome; Single molecule; Translation; Translocation

Indexed keywords

RIBOSOME PROTEIN;

EID: 77149151868     PISSN: 02614189     EISSN: 14602075     Source Type: Journal    
DOI: 10.1038/emboj.2009.384     Document Type: Article
Times cited : (67)

References (56)
  • 1
    • 54049116765 scopus 로고    scopus 로고
    • Visualization of the hybrid state of tRNA binding promoted by spontaneous ratcheting of the ribosome
    • Agirrezabala X, Lei J, Brunelle JL, Ortiz-Meoz RF, Green R, Frank J (2008) Visualization of the hybrid state of tRNA binding promoted by spontaneous ratcheting of the ribosome. Mol Cell 32: 190-197
    • (2008) Mol Cell , vol.32 , pp. 190-197
    • Agirrezabala, X.1    Lei, J.2    Brunelle, J.L.3    Ortiz-Meoz, R.F.4    Green, R.5    Frank, J.6
  • 3
    • 0021112855 scopus 로고
    • Spontaneous, elongation factor G independent translocation of Escherichia coli ribosomes
    • Bergemann K, Nierhaus KH (1983) Spontaneous, elongation factor G independent translocation of Escherichia coli ribosomes. J Biol Chem 258: 15105-15113
    • (1983) J Biol Chem , vol.258 , pp. 15105-15113
    • Bergemann, K.1    Nierhaus, K.H.2
  • 10
    • 44449125068 scopus 로고    scopus 로고
    • Spontaneous intersubunit rotation in single ribosomes
    • Cornish PV, Ermolenko DN, Noller HF, Ha T (2008) Spontaneous intersubunit rotation in single ribosomes. Mol Cell 30: 578-588
    • (2008) Mol Cell , vol.30 , pp. 578-588
    • Cornish, P.V.1    Ermolenko, D.N.2    Noller, H.F.3    Ha, T.4
  • 13
    • 0042173407 scopus 로고    scopus 로고
    • Ribosomal proteins S12 and S13 function as control elements for translocation of the mRNA-tRNA complex
    • Cukras AR, Southworth DR, Brunelle JL, Culver GM, Green R (2003) Ribosomal proteins S12 and S13 function as control elements for translocation of the mRNA-tRNA complex. Mol Cell 12: 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
  • 14
    • 66149152243 scopus 로고    scopus 로고
    • Mitigating unwanted photophysical processes for improved single-molecule fluorescence imaging
    • Dave R, Terry DS, Munro JB, Blanchard SC (2009) Mitigating unwanted photophysical processes for improved single-molecule fluorescence imaging. Biophys J 96: 2371-2381
    • (2009) Biophys J , vol.96 , pp. 2371-2381
    • Dave, R.1    Terry, D.S.2    Munro, J.B.3    Blanchard, S.C.4
  • 15
    • 33644798018 scopus 로고    scopus 로고
    • The hybrid state of tRNA binding is an authentic translation elongation intermediate
    • Dorner S, Brunelle JL, Sharma D, Green R (2006) The hybrid state of tRNA binding is an authentic translation elongation intermediate. Nat Struct Mol Biol 13: 234-241
    • (2006) Nat Struct Mol Biol , vol.13 , pp. 234-241
    • Dorner, S.1    Brunelle, J.L.2    Sharma, D.3    Green, R.4
  • 17
    • 42949126723 scopus 로고    scopus 로고
    • Coupling of ribosomal L1 stalk and tRNA dynamics during translation elongation
    • Fei J, Kosuri P, MacDougall DD, Gonzalez Jr RL (2008) Coupling of ribosomal L1 stalk and tRNA dynamics during translation elongation. Mol Cell 30: 348-359
    • (2008) Mol Cell , vol.30 , pp. 348-359
    • Fei, J.1    Kosuri, P.2    MacDougall, D.D.3    Gonzalez Jr, R.L.4
  • 19
    • 0038286524 scopus 로고    scopus 로고
    • Catalysis of ribosomal translocation by sparsomycin
    • Fredrick K, Noller H (2003) Catalysis of ribosomal translocation by sparsomycin. Science 300: 1159-1162
    • (2003) Science , vol.300 , pp. 1159-1162
    • Fredrick, K.1    Noller, H.2
  • 20
    • 70350602056 scopus 로고    scopus 로고
    • The structure of the ribosome with elongation factor G trapped in the posttranslocational state
    • Gao YG, Selmer M, Dunham CM, Weixlbaumer A, Kelley AC, Ramakrishnan V (2009) The structure of the ribosome with elongation factor G trapped in the posttranslocational state. Science 326: 694-699
    • (2009) Science , vol.326 , pp. 694-699
    • Gao, Y.G.1    Selmer, M.2    Dunham, C.M.3    Weixlbaumer, A.4    Kelley, A.C.5    Ramakrishnan, V.6
  • 21
    • 84886634813 scopus 로고
    • Factor-free ('non-enzymic') and factor-dependent systems of translation of polyuridylic acid by Escherichia coli ribosomes
    • Gavrilova LP, Kostiashkina OE, Koteliansky VE, Rutkevitch NM, Spirin AS (1976) Factor-free ('non-enzymic') and factor-dependent systems of translation of polyuridylic acid by Escherichia coli ribosomes. J Mol Biol 101: 537-552
    • (1976) J Mol Biol , vol.101 , pp. 537-552
    • Gavrilova, L.P.1    Kostiashkina, O.E.2    Koteliansky, V.E.3    Rutkevitch, N.M.4    Spirin, A.S.5
  • 22
    • 23644451172 scopus 로고    scopus 로고
    • Crystal structure of a mutant elongation factor G trapped with a GTP analogue
    • Hansson S, Singh R, Gudkov AT, Liljas A, Logan DT (2005) Crystal structure of a mutant elongation factor G trapped with a GTP analogue. FEBS Lett 579: 4492-4497
    • (2005) FEBS Lett , vol.579 , pp. 4492-4497
    • Hansson, S.1    Singh, R.2    Gudkov, A.T.3    Liljas, A.4    Logan, D.T.5
  • 24
    • 4143071283 scopus 로고    scopus 로고
    • Single-molecule three-color FRET
    • Hohng S, Joo C, Ha T (2004) Single-molecule three-color FRET. Biophys J 87: 1328-1337
    • (2004) Biophys J , vol.87 , pp. 1328-1337
    • Hohng, S.1    Joo, C.2    Ha, T.3
  • 25
    • 34247584538 scopus 로고    scopus 로고
    • Intersubunit movement is required for ribosomal translocation
    • Horan LH, Noller HF (2007) Intersubunit movement is required for ribosomal translocation. Proc Natl Acad Sci USA 104: 4881-4885
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 4881-4885
    • Horan, L.H.1    Noller, H.F.2
  • 27
    • 33748582906 scopus 로고    scopus 로고
    • Crystal structure of a 70S ribosome-tRNA complex reveals functional interactions and rearrangements
    • Korostelev A, Trakhanov S, Laurberg M, Noller HF (2006) Crystal structure of a 70S ribosome-tRNA complex reveals functional interactions and rearrangements. Cell 126: 1065-1077
    • (2006) Cell , vol.126 , pp. 1065-1077
    • Korostelev, A.1    Trakhanov, S.2    Laurberg, M.3    Noller, H.F.4
  • 28
    • 33750639677 scopus 로고
    • The key-lock theory and the induced fit theory
    • Koshland Jr DE (1995) The key-lock theory and the induced fit theory. Angew Chem Int Ed Engl 33: 2375-2378
    • (1995) Angew Chem Int Ed Engl , vol.33 , pp. 2375-2378
    • Koshland Jr, D.E.1
  • 29
    • 0035838382 scopus 로고    scopus 로고
    • Current topics in RNA-protein recognition: Control of specificity and biological function through induced fit and conformational capture
    • Leulliot N, Varani G (2001) Current topics in RNA-protein recognition: control of specificity and biological function through induced fit and conformational capture. Biochemistry 40: 7947-7956
    • (2001) Biochemistry , vol.40 , pp. 7947-7956
    • Leulliot, N.1    Varani, G.2
  • 30
    • 67649646602 scopus 로고    scopus 로고
    • GTP hydrolysis by IF2 guides progression of the ribosome into elongation
    • Marshall RA, Aitken CE, Puglisi JD (2009) GTP hydrolysis by IF2 guides progression of the ribosome into elongation. Mol Cell 35: 37-47
    • (2009) Mol Cell , vol.35 , pp. 37-47
    • Marshall, R.A.1    Aitken, C.E.2    Puglisi, J.D.3
  • 31
    • 77149140812 scopus 로고    scopus 로고
    • Translational Control in Biology and Medicine, Mathews MB, Sonenberg N, Hershey JW (eds) Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • Mathews MB, Sonenberg N, Hershey JW (2007) Origins and principles of translational control. In Translational Control in Biology and Medicine, Mathews MB, Sonenberg N, Hershey JW (eds). pp 1-40. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press
    • (2007) Origins and Principles of Translational Control , pp. 1-40
    • Mathews, M.B.1    Sonenberg, N.2    Hershey, J.W.3
  • 32
    • 0024458904 scopus 로고
    • Intermediate states in the movement of transfer RNA in the ribosome
    • Moazed D, Noller HF (1989) Intermediate states in the movement of transfer RNA in the ribosome. Nature 342: 142-148
    • (1989) Nature , vol.342 , pp. 142-148
    • Moazed, D.1    Noller, H.F.2
  • 33
    • 33847051154 scopus 로고    scopus 로고
    • Identification of two distinct hybrid state intermediates on the ribosome
    • Munro JB, Altman RB, O'Connor N, Blanchard SC (2007) Identification of two distinct hybrid state intermediates on the ribosome. Mol Cell 25: 505-517
    • (2007) Mol Cell , vol.25 , pp. 505-517
    • Munro, J.B.1    Altman, R.B.2    O'Connor, N.3    Blanchard, S.C.4
  • 36
    • 33847024820 scopus 로고    scopus 로고
    • Kinetically competent intermediates in the translocation step of protein synthesis
    • Pan D, Kirillov S, Cooperman BS (2007) Kinetically competent intermediates in the translocation step of protein synthesis. Mol Cell 25: 519-529
    • (2007) Mol Cell , vol.25 , pp. 519-529
    • Pan, D.1    Kirillov, S.2    Cooperman, B.S.3
  • 37
    • 6344252614 scopus 로고    scopus 로고
    • Conformational changes of the small ribosomal subunit during elongation factor G-dependent tRNA-mRNA transloca-tion
    • Peske F, Savelsbergh A, Katunin VI, Rodnina MV, Wintermeyer W (2004) Conformational changes of the small ribosomal subunit during elongation factor G-dependent tRNA-mRNA transloca-tion. J Mol Biol 343: 1183-1194
    • (2004) J Mol Biol , vol.343 , pp. 1183-1194
    • Peske, F.1    Savelsbergh, A.2    Katunin, V.I.3    Rodnina, M.V.4    Wintermeyer, W.5
  • 38
    • 1542285356 scopus 로고    scopus 로고
    • Restoration of single-channel currents using the segmental k-means method based on hidden Markov modeling
    • Qin F (2004) Restoration of single-channel currents using the segmental k-means method based on hidden Markov modeling. Biophys J 86: 1488-1501
    • (2004) Biophys J , vol.86 , pp. 1488-1501
    • Qin, F.1
  • 39
    • 0030061670 scopus 로고    scopus 로고
    • Estimating single-channel kinetic parameters from idealized patch-clamp data containing missed events
    • Qin F, Auerbach A, Sachs F (1996) Estimating single-channel kinetic parameters from idealized patch-clamp data containing missed events. Biophys J 70: 264-280
    • (1996) Biophys J , vol.70 , pp. 264-280
    • Qin, F.1    Auerbach, A.2    Sachs, F.3
  • 40
    • 0031028688 scopus 로고    scopus 로고
    • Hydrolysis of GTP by elongation factor G drives tRNA movement on the ribosome
    • Rodnina MV, Savelsbergh A, Katunin VI, Wintermeyer W (1997) Hydrolysis of GTP by elongation factor G drives tRNA movement on the ribosome. Nature 385: 37-41
    • (1997) Nature , vol.385 , pp. 37-41
    • Rodnina, M.V.1    Savelsbergh, A.2    Katunin, V.I.3    Wintermeyer, W.4
  • 42
  • 43
    • 65249164177 scopus 로고    scopus 로고
    • Distinct functions of elongation factor G in ribosome recycling and transloca-tion
    • Savelsbergh A, Rodnina MV, Wintermeyer W (2009) Distinct functions of elongation factor G in ribosome recycling and transloca-tion. RNA 15: 772-780
    • (2009) RNA , vol.15 , pp. 772-780
    • Savelsbergh, A.1    Rodnina, M.V.2    Wintermeyer, W.3
  • 46
    • 0346362324 scopus 로고    scopus 로고
    • EF-G-independent reactivity of a pre-translocation-state ribosome complex with the aminoacyl tRNA substrate puromycin supports an intermediate (hybrid) state of tRNA binding
    • Sharma D, Southworth DR, Green R (2004) EF-G-independent reactivity of a pre-translocation-state ribosome complex with the aminoacyl tRNA substrate puromycin supports an intermediate (hybrid) state of tRNA binding. RNA 10: 102-113
    • (2004) RNA , vol.10 , pp. 102-113
    • Sharma, D.1    Southworth, D.R.2    Green, R.3
  • 47
    • 65249132345 scopus 로고    scopus 로고
    • Ribosomal translocation: One step closer to the molecular mechanism
    • Shoji S, Walker SE, Fredrick K (2009) Ribosomal translocation: one step closer to the molecular mechanism. ACS Chem Biol 4: 93-107
    • (2009) ACS Chem Biol , vol.4 , pp. 93-107
    • Shoji, S.1    Walker, S.E.2    Fredrick, K.3
  • 48
    • 34548339675 scopus 로고    scopus 로고
    • Elongation factor G stabilizes the hybrid-state conformation of the 70S ribosome
    • Spiegel PC, Ermolenko DN, Noller HF (2007) Elongation factor G stabilizes the hybrid-state conformation of the 70S ribosome. RNA 13: 1473-1482
    • (2007) RNA , vol.13 , pp. 1473-1482
    • Spiegel, P.C.1    Ermolenko, D.N.2    Noller, H.F.3
  • 49
    • 67651178174 scopus 로고    scopus 로고
    • The ribosome as a conveying thermal ratchet machine
    • Spirin AS (2009) The ribosome as a conveying thermal ratchet machine. J Biol Chem 284: 21103-21119
    • (2009) J Biol Chem , vol.284 , pp. 21103-21119
    • Spirin, A.S.1
  • 50
    • 68249151083 scopus 로고    scopus 로고
    • Translation factors direct intrinsic ribosome dynamics during translation termination and ribosome recycling
    • Sternberg SH, Fei J, Prywes N, McGrath KA, Gonzalez Jr RL (2009) Translation factors direct intrinsic ribosome dynamics during translation termination and ribosome recycling. Nat Struct Mol Biol 16: 861-868
    • (2009) Nat Struct Mol Biol , vol.16 , pp. 861-868
    • Sternberg, S.H.1    Fei, J.2    Prywes, N.3    McGrath, K.A.4    Gonzalez Jr, R.L.5
  • 51
    • 34247560812 scopus 로고    scopus 로고
    • Structures of modified eEF2.80S ribosome complexes reveal the role of GTP hydrolysis in translocation
    • Taylor DJ, Nilsson J, Merrill AR, Andersen GR, Nissen P, Frank J (2007) Structures of modified eEF2.80S ribosome complexes reveal the role of GTP hydrolysis in translocation. EMBO J 26: 2421-2431
    • (2007) EMBO J , vol.26 , pp. 2421-2431
    • Taylor, D.J.1    Nilsson, J.2    Merrill, A.R.3    Andersen, G.R.4    Nissen, P.5    Frank, J.6
  • 52
    • 0036786684 scopus 로고    scopus 로고
    • All-atom homology model of the Escherichia coli 30S ribosomal subunit
    • Tung C, Joseph S, Sanbonmatsu K (2002) All-atom homology model of the Escherichia coli 30S ribosomal subunit. Nat Struct Biol 9: 750-755
    • (2002) Nat Struct Biol , vol.9 , pp. 750-755
    • Tung, C.1    Joseph, S.2    Sanbonmatsu, K.3
  • 56
    • 0038300651 scopus 로고    scopus 로고
    • Peptidyl-tRNA regulates the GTPase activity of translation factors
    • Zavialov AV, Ehrenberg M (2003) Peptidyl-tRNA regulates the GTPase activity of translation factors. Cell 114: 113-122
    • (2003) Cell , vol.114 , pp. 113-122
    • Zavialov, A.V.1    Ehrenberg, M.2


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