메뉴 건너뛰기




Volumn 15, Issue 6, 2011, Pages 853-863

In vitro and in vivo single-molecule fluorescence imaging of ribosome-catalyzed protein synthesis

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; ESCHERICHIA COLI; FLUORESCENCE; GENE EXPRESSION; IN VITRO STUDY; IN VIVO STUDY; KINETICS; NONHUMAN; PROTEIN STRUCTURE; PROTEIN SYNTHESIS; REVIEW; RIBOSOME; SINGLE MOLECULE FLUORESCENCE; BIOCATALYSIS; CHEMICAL STRUCTURE; CHEMISTRY; EQUIPMENT; FLUORESCENCE MICROSCOPY; FLUORESCENCE RESONANCE ENERGY TRANSFER; GENETICS; METABOLISM; METHODOLOGY; PHYSIOLOGY; STAINING; ULTRASTRUCTURE;

EID: 83055186409     PISSN: 13675931     EISSN: 18790402     Source Type: Journal    
DOI: 10.1016/j.cbpa.2011.11.002     Document Type: Review
Times cited : (14)

References (76)
  • 1
    • 70350654363 scopus 로고    scopus 로고
    • What recent ribosome structures have revealed about the mechanism of translation
    • Schmeing T.M., Ramakrishnan V. What recent ribosome structures have revealed about the mechanism of translation. Nature 2009, 461:1234-1242.
    • (2009) Nature , vol.461 , pp. 1234-1242
    • Schmeing, T.M.1    Ramakrishnan, V.2
  • 5
    • 79959655626 scopus 로고    scopus 로고
    • Biological mechanisms, one molecule at a time
    • Tinoco I., Gonzalez R.L. Biological mechanisms, one molecule at a time. Gene Dev 2011, 25:1205-1231.
    • (2011) Gene Dev , vol.25 , pp. 1205-1231
    • Tinoco, I.1    Gonzalez, R.L.2
  • 10
    • 0028945654 scopus 로고
    • Imaging of single fluorescent molecules and individual ATP turnovers by single myosin molecules in aqueous solution
    • Funatsu T., Harada Y., Tokunaga M., Saito K., Yanagida T. Imaging of single fluorescent molecules and individual ATP turnovers by single myosin molecules in aqueous solution. Nature 1995, 374:555-559.
    • (1995) Nature , vol.374 , pp. 555-559
    • Funatsu, T.1    Harada, Y.2    Tokunaga, M.3    Saito, K.4    Yanagida, T.5
  • 13
    • 0001973896 scopus 로고
    • Regulation of biosynthesis of ribosomes
    • Cold Spring Harbor Laboratory Press, M. Nomura, A. Tissieres, P. Lengyel (Eds.)
    • Kjeldgaard N.O., Gausing K. Regulation of biosynthesis of ribosomes. Ribosomes 1974, Cold Spring Harbor Laboratory Press. M. Nomura, A. Tissieres, P. Lengyel (Eds.).
    • (1974) Ribosomes
    • Kjeldgaard, N.O.1    Gausing, K.2
  • 14
    • 0017389047 scopus 로고
    • Transcription and translation initiation frequencies of the Escherichia coli lac operon
    • Kennell D., Riezman H. Transcription and translation initiation frequencies of the Escherichia coli lac operon. J Mol Biol 1977, 114:1-21.
    • (1977) J Mol Biol , vol.114 , pp. 1-21
    • Kennell, D.1    Riezman, H.2
  • 16
    • 80054772954 scopus 로고    scopus 로고
    • Real-time single-molecule observation of green fluorescent protein synthesis by immobilized ribosomes
    • Iizuka R., Funatsu T., Uemura S. Real-time single-molecule observation of green fluorescent protein synthesis by immobilized ribosomes. Methods Mol Biol 2011, 778:215-228.
    • (2011) Methods Mol Biol , vol.778 , pp. 215-228
    • Iizuka, R.1    Funatsu, T.2    Uemura, S.3
  • 18
    • 60149099539 scopus 로고    scopus 로고
    • Fidelity at the molecular level: lessons from protein synthesis
    • Zaher H.S., Green R. Fidelity at the molecular level: lessons from protein synthesis. Cell 2009, 136:746-762.
    • (2009) Cell , vol.136 , pp. 746-762
    • Zaher, H.S.1    Green, R.2
  • 19
    • 77953625418 scopus 로고    scopus 로고
    • Structure and dynamics of a processive Brownian motor: the translating ribosome
    • Frank J., Gonzalez R.L. Structure and dynamics of a processive Brownian motor: the translating ribosome. Ann Rev Biochem 2010, 79:381-412.
    • (2010) Ann Rev Biochem , vol.79 , pp. 381-412
    • Frank, J.1    Gonzalez, R.L.2
  • 20
    • 34247589630 scopus 로고    scopus 로고
    • The ribosomal peptidyl transferase
    • Beringer M., Rodnina M.V. The ribosomal peptidyl transferase. Mol Cell 2007, 26:311-321.
    • (2007) Mol Cell , vol.26 , pp. 311-321
    • Beringer, M.1    Rodnina, M.V.2
  • 22
    • 79953199843 scopus 로고    scopus 로고
    • The ribosome as a molecular machine: the mechanism of tRNA-mRNA movement in translocation
    • Rodnina M.V., Wintermeyer W. The ribosome as a molecular machine: the mechanism of tRNA-mRNA movement in translocation. Biochem Soc Trans 2011, 39:658-662.
    • (2011) Biochem Soc Trans , vol.39 , pp. 658-662
    • Rodnina, M.V.1    Wintermeyer, W.2
  • 24
    • 55749099506 scopus 로고    scopus 로고
    • Irreversible chemical steps control intersubunit dynamics during translation
    • Marshall R.A., Dorywalska M., Puglisi J.D. Irreversible chemical steps control intersubunit dynamics during translation. Proc Natl Acad Sci U S A 2008, 105:15364-15369.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 15364-15369
    • Marshall, R.A.1    Dorywalska, M.2    Puglisi, J.D.3
  • 25
    • 77954383845 scopus 로고    scopus 로고
    • Following the intersubunit conformation of the ribosome during translation in real time
    • Aitken C.E., Puglisi J.D. Following the intersubunit conformation of the ribosome during translation in real time. Nat Struct Mol Biol 2010, 17:793-800.
    • (2010) Nat Struct Mol Biol , vol.17 , pp. 793-800
    • Aitken, C.E.1    Puglisi, J.D.2
  • 26
    • 0034807927 scopus 로고    scopus 로고
    • Single-molecule fluorescence resonance energy transfer
    • Ha T. Single-molecule fluorescence resonance energy transfer. Methods 2001, 25:78-86.
    • (2001) Methods , vol.25 , pp. 78-86
    • Ha, T.1
  • 27
    • 50649121477 scopus 로고    scopus 로고
    • Advances in single-molecule fluorescence methods for molecular biology
    • Joo C., Balci H., Ishitsuka Y., Buranachai C., Ha T. Advances in single-molecule fluorescence methods for molecular biology. Ann Rev Biochem 2008, 77:51-76.
    • (2008) Ann Rev Biochem , vol.77 , pp. 51-76
    • Joo, C.1    Balci, H.2    Ishitsuka, Y.3    Buranachai, C.4    Ha, T.5
  • 29
    • 53349152992 scopus 로고    scopus 로고
    • Zero-mode waveguides: sub-wavelength nanostructures for single molecule studies at high concentrations
    • Moran-Mirabal J.M., Craighead H.G. Zero-mode waveguides: sub-wavelength nanostructures for single molecule studies at high concentrations. Methods 2008, 46:11-17.
    • (2008) Methods , vol.46 , pp. 11-17
    • Moran-Mirabal, J.M.1    Craighead, H.G.2
  • 31
    • 0025036111 scopus 로고
    • Ribosome gymnastics-degree of difficulty 9.5, style 10.0
    • Atkins J.F., Weiss R.B., Gesteland R.F. Ribosome gymnastics-degree of difficulty 9.5, style 10.0. Cell 1990, 62:413-423.
    • (1990) Cell , vol.62 , pp. 413-423
    • Atkins, J.F.1    Weiss, R.B.2    Gesteland, R.F.3
  • 34
    • 36248958685 scopus 로고    scopus 로고
    • Thiostrepton inhibition of tRNA delivery to the ribosome
    • Gonzalez R.L., Chu S., Puglisi J.D. Thiostrepton inhibition of tRNA delivery to the ribosome. RNA 2007, 13:2091-2097.
    • (2007) RNA , vol.13 , pp. 2091-2097
    • Gonzalez, R.L.1    Chu, S.2    Puglisi, J.D.3
  • 36
    • 77952717308 scopus 로고    scopus 로고
    • Accommodation of aminoacyl-tRNA into the ribosome involves reversible excursions along multiple pathways
    • Whitford P.C., Geggier P., Altman R.B., Blanchard S.C., Onuchic J.N., Sanbonmatsu K.Y. Accommodation of aminoacyl-tRNA into the ribosome involves reversible excursions along multiple pathways. RNA 2010, 16:1196-1204.
    • (2010) RNA , vol.16 , pp. 1196-1204
    • Whitford, P.C.1    Geggier, P.2    Altman, R.B.3    Blanchard, S.C.4    Onuchic, J.N.5    Sanbonmatsu, K.Y.6
  • 38
    • 78649774217 scopus 로고    scopus 로고
    • Codon-dependent tRNA fluctuations monitored with fluorescence polarization
    • Mishra P.P., Qureshi M.T., Ren W.R., Lee T.H. Codon-dependent tRNA fluctuations monitored with fluorescence polarization. Biophys J 2010, 99:3849-3858.
    • (2010) Biophys J , vol.99 , pp. 3849-3858
    • Mishra, P.P.1    Qureshi, M.T.2    Ren, W.R.3    Lee, T.H.4
  • 40
    • 33847051154 scopus 로고    scopus 로고
    • Identification of two distinct hybrid state intermediates on the ribosome
    • Munro J.B., Altman R.B., O'Connor N., Blanchard S.C. Identification of two distinct hybrid state intermediates on the ribosome. Mol Cell 2007, 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
  • 42
    • 36549020733 scopus 로고    scopus 로고
    • Fluctuations of transfer RNAs between classical and hybrid states
    • Kim H.D., Puglisi J., Chu S. Fluctuations of transfer RNAs between classical and hybrid states. Biophys J 2007, 93:3575-3582.
    • (2007) Biophys J , vol.93 , pp. 3575-3582
    • Kim, H.D.1    Puglisi, J.2    Chu, S.3
  • 43
    • 42949126723 scopus 로고    scopus 로고
    • Coupling of ribosomal L1 stalk and tRNA dynamics during translation elongation
    • Fei J., Kosuri P., MacDougall D.D., Gonzalez R.L. Coupling of ribosomal L1 stalk and tRNA dynamics during translation elongation. Mol Cell 2008, 30:348-359.
    • (2008) Mol Cell , vol.30 , pp. 348-359
    • Fei, J.1    Kosuri, P.2    MacDougall, D.D.3    Gonzalez, R.L.4
  • 44
    • 44449125068 scopus 로고    scopus 로고
    • Spontaneous intersubunit rotation in single ribosomes
    • Cornish P.V., Ermolenko D.N., Noller H.F., Ha T. Spontaneous intersubunit rotation in single ribosomes. Mol Cell 2008, 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
  • 46
    • 70349470607 scopus 로고    scopus 로고
    • Allosteric collaboration between elongation factor G and the ribosomal L1 stalk directs tRNA movements during translation
    • Fei J., Bronson J.E., Hofman J.M., Srinivas R.L., Wiggins C.H., Gonzalez R.L.J. Allosteric collaboration between elongation factor G and the ribosomal L1 stalk directs tRNA movements during translation. Proc Natl Acad Sci U S A 2009, 106:15702-15707.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 15702-15707
    • Fei, J.1    Bronson, J.E.2    Hofman, J.M.3    Srinivas, R.L.4    Wiggins, C.H.5    Gonzalez, R.L.J.6
  • 48
    • 77950391683 scopus 로고    scopus 로고
    • Aminoglycoside activity observed on single pre-translocation ribosome complexes
    • Feldman M.B., Terry D.S., Altman R.B., Blanchard S.C. Aminoglycoside activity observed on single pre-translocation ribosome complexes. Nat Chem Biol 2010, 6:54-62.
    • (2010) Nat Chem Biol , vol.6 , pp. 54-62
    • Feldman, M.B.1    Terry, D.S.2    Altman, R.B.3    Blanchard, S.C.4
  • 50
    • 78149455739 scopus 로고    scopus 로고
    • Single-molecule study of ribosome hierarchic dynamics at the peptidyl transferase center
    • Altuntop M.E., Ly C.T., Wang Y. Single-molecule study of ribosome hierarchic dynamics at the peptidyl transferase center. Biophys J 2010, 99:3002-3009.
    • (2010) Biophys J , vol.99 , pp. 3002-3009
    • Altuntop, M.E.1    Ly, C.T.2    Wang, Y.3
  • 51
    • 78149443288 scopus 로고    scopus 로고
    • Single-molecule study of viomycin's inhibition mechanism on ribosome translocation
    • Ly C.T., Altuntop M.E., Wang Y.H. Single-molecule study of viomycin's inhibition mechanism on ribosome translocation. Biochemistry 2010, 49:9732-9738.
    • (2010) Biochemistry , vol.49 , pp. 9732-9738
    • Ly, C.T.1    Altuntop, M.E.2    Wang, Y.H.3
  • 53
    • 78650409178 scopus 로고    scopus 로고
    • A microfluidic approach for investigating the temperature dependence of biomolecular activity with single-molecule resolution
    • Wang B., Ho J., Fei J., Gonzalez R.L., Lin Q. A microfluidic approach for investigating the temperature dependence of biomolecular activity with single-molecule resolution. Lab Chip 2011, 11:274-281.
    • (2011) Lab Chip , vol.11 , pp. 274-281
    • Wang, B.1    Ho, J.2    Fei, J.3    Gonzalez, R.L.4    Lin, Q.5
  • 55
    • 80052446046 scopus 로고    scopus 로고
    • Transfer RNA-mediated regulation of ribosome dynamics during protein synthesis
    • Fei J., Richard A.C., Bronson J.E., Gonzalez R.L. Transfer RNA-mediated regulation of ribosome dynamics during protein synthesis. Nat Struct Mol Biol 2011, 18:1043-1106.
    • (2011) Nat Struct Mol Biol , vol.18 , pp. 1043-1106
    • Fei, J.1    Richard, A.C.2    Bronson, J.E.3    Gonzalez, R.L.4
  • 56
    • 67649646602 scopus 로고    scopus 로고
    • GTP hydrolysis by IF2 guides progression of the ribosome into elongation
    • Marshall R.A., Aitken C.E., Puglisi J.D. GTP hydrolysis by IF2 guides progression of the ribosome into elongation. Mol Cell 2009, 35:37-47.
    • (2009) Mol Cell , vol.35 , pp. 37-47
    • Marshall, R.A.1    Aitken, C.E.2    Puglisi, J.D.3
  • 57
    • 68249151083 scopus 로고    scopus 로고
    • Translation factors direct intrinsic ribosome dynamics during translation termination and ribosome recycling
    • Sternberg S.H., Fei J., Prywes N., McGrath K.A., Gonzalez R.L. Translation factors direct intrinsic ribosome dynamics during translation termination and ribosome recycling. Nat Struct Mol Biol 2009, 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, R.L.5
  • 59
    • 53849146066 scopus 로고    scopus 로고
    • Peptide release on the ribosome: mechanism and implications for translational control
    • Youngman E.A., McDonald M.E., Green R. Peptide release on the ribosome: mechanism and implications for translational control. Annu Rev Microbiol 2008, 62:353-373.
    • (2008) Annu Rev Microbiol , vol.62 , pp. 353-373
    • Youngman, E.A.1    McDonald, M.E.2    Green, R.3
  • 61
    • 66549108297 scopus 로고    scopus 로고
    • Structure-function insights into prokaryotic and eukaryotic translation initiation
    • Myasnikov A.G., Simonetti A., Marzi S., Klaholz B.P. Structure-function insights into prokaryotic and eukaryotic translation initiation. Curr Opin Struct Biol 2009, 19:300-309.
    • (2009) Curr Opin Struct Biol , vol.19 , pp. 300-309
    • Myasnikov, A.G.1    Simonetti, A.2    Marzi, S.3    Klaholz, B.P.4
  • 62
    • 77749322692 scopus 로고    scopus 로고
    • Structural and mechanistic insights into translation termination
    • Loh P.G., Song H.W. Structural and mechanistic insights into translation termination. Curr Opin Struct Biol 2010, 20:98-103.
    • (2010) Curr Opin Struct Biol , vol.20 , pp. 98-103
    • Loh, P.G.1    Song, H.W.2
  • 63
    • 78649508041 scopus 로고    scopus 로고
    • Role of the initiation factors in mRNA start site selection and fMet-tRNA recruitment by bacterial ribosomes
    • Gualerzi C.O., Fabbretti A., Brandi L., Milon P., Pon C.L. Role of the initiation factors in mRNA start site selection and fMet-tRNA recruitment by bacterial ribosomes. Israel J Chem 2010, 50:80-94.
    • (2010) Israel J Chem , vol.50 , pp. 80-94
    • Gualerzi, C.O.1    Fabbretti, A.2    Brandi, L.3    Milon, P.4    Pon, C.L.5
  • 64
    • 79955662779 scopus 로고    scopus 로고
    • Molecular recognition and catalysis in translation termination complexes
    • Klaholz B.P. Molecular recognition and catalysis in translation termination complexes. TIBS 2011, 36:282-292.
    • (2011) TIBS , vol.36 , pp. 282-292
    • Klaholz, B.P.1
  • 65
    • 79960471842 scopus 로고    scopus 로고
    • Structural aspects of translation termination on the ribosome
    • Korostelev A.A. Structural aspects of translation termination on the ribosome. RNA 2011, 17:1409-1421.
    • (2011) RNA , vol.17 , pp. 1409-1421
    • Korostelev, A.A.1
  • 66
    • 56749104130 scopus 로고    scopus 로고
    • Fluorescent probes for super-resolution imaging in living cells
    • Fernandez-Suarez M., Ting A.Y. Fluorescent probes for super-resolution imaging in living cells. Nat Rev Mol Cell Biol 2008, 9:929-943.
    • (2008) Nat Rev Mol Cell Biol , vol.9 , pp. 929-943
    • Fernandez-Suarez, M.1    Ting, A.Y.2
  • 67
    • 78349313682 scopus 로고    scopus 로고
    • How to obtain labeled proteins and what to do with them
    • Hinner M.J., Johnsson K. How to obtain labeled proteins and what to do with them. Curr Opin Biotech 2010, 21:766-776.
    • (2010) Curr Opin Biotech , vol.21 , pp. 766-776
    • Hinner, M.J.1    Johnsson, K.2
  • 68
    • 33645027986 scopus 로고    scopus 로고
    • Stochastic protein expression in individual cells at the single molecule level
    • Cai L., Friedman N., Xie X.S. Stochastic protein expression in individual cells at the single molecule level. Nature 2006, 440:358-362.
    • (2006) Nature , vol.440 , pp. 358-362
    • Cai, L.1    Friedman, N.2    Xie, X.S.3
  • 69
    • 33645033645 scopus 로고    scopus 로고
    • Probing gene expression in live cells, one protein molecule at a time
    • Yu J., Xiao J., Ren X., Lao K., Xie X.S. Probing gene expression in live cells, one protein molecule at a time. Science 2006, 311:1600-1603.
    • (2006) Science , vol.311 , pp. 1600-1603
    • Yu, J.1    Xiao, J.2    Ren, X.3    Lao, K.4    Xie, X.S.5
  • 70
    • 77955102352 scopus 로고    scopus 로고
    • Quantifying E. coli proteome and transcriptome with single-molecule sensitivity in single cells
    • Taniguchi Y., Choi P.J., Li G.W., Chen H., Babu M., Hearn J., Emili A., Xie X.S. Quantifying E. coli proteome and transcriptome with single-molecule sensitivity in single cells. Science 2010, 329:533-538.
    • (2010) Science , vol.329 , pp. 533-538
    • Taniguchi, Y.1    Choi, P.J.2    Li, G.W.3    Chen, H.4    Babu, M.5    Hearn, J.6    Emili, A.7    Xie, X.S.8
  • 74
    • 78649426085 scopus 로고    scopus 로고
    • Crystal structure of the eukaryotic ribosome
    • Ben-Shem A., Jenner L., Yusupova G., Yusupov M. Crystal structure of the eukaryotic ribosome. Science 2010, 330:1203-1209.
    • (2010) Science , vol.330 , pp. 1203-1209
    • Ben-Shem, A.1    Jenner, L.2    Yusupova, G.3    Yusupov, M.4
  • 75
    • 77955233802 scopus 로고    scopus 로고
    • Site-specific labeling of Saccharomyces cerevisiae ribosomes for single-molecule manipulations
    • Petrov A., Puglisi J.D. Site-specific labeling of Saccharomyces cerevisiae ribosomes for single-molecule manipulations. Nucleic Acids Res 2010, 38:e143.
    • (2010) Nucleic Acids Res , vol.38
    • Petrov, A.1    Puglisi, J.D.2
  • 76
    • 75149196287 scopus 로고    scopus 로고
    • The mechanism of eukaryotic translation initiation and principles of its regulation
    • Jackson R.J., Hellen C.U.T., Pestova T.V. The mechanism of eukaryotic translation initiation and principles of its regulation. Nat Rev Mol Cell Biol 2010, 11:113-127.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 113-127
    • Jackson, R.J.1    Hellen, C.U.T.2    Pestova, T.V.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.