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Volumn 114, Issue 1, 2003, Pages 123-134

Locking and unlocking of ribosomal motions

Author keywords

[No Author keywords available]

Indexed keywords

ELONGATION FACTOR G; MESSENGER RNA; TRANSFER RNA;

EID: 0037963475     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(03)00476-8     Document Type: Article
Times cited : (538)

References (48)
  • 1
    • 0032568584 scopus 로고    scopus 로고
    • Visualization of elongation factor G on the Escherichia coli 70S ribosome: The mechanism of translocation
    • Agrawal R.K., Penzeck P., Grassucci R.A., Frank J. Visualization of elongation factor G on the Escherichia coli 70S ribosome. the mechanism of translocation Proc. Natl. Acad. Sci. USA. 95:1998;6134-6138.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 6134-6138
    • Agrawal, R.K.1    Penzeck, P.2    Grassucci, R.A.3    Frank, J.4
  • 2
    • 0032982866 scopus 로고    scopus 로고
    • EF-G-dependent GTP hydrolysis induces translocation accompanied by large conformational changes in the 70S ribosome
    • Agrawal R.K., Heagle A.B., Penzeck P., Grassucci R.A., Frank J. 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    Penzeck, P.3    Grassucci, R.A.4    Frank, J.5
  • 3
    • 0002318277 scopus 로고    scopus 로고
    • Studies of elongation factor G-dependent tRNA translocation by three-dimensional cryoelectron microscopy
    • R.A. Garret, S.R. Douthwaite, A. Liljas, T. Matheson, P.B. Moore, & H.F. Noller. Washington, D.C.: ASM Press. a
    • Agrawal R.K., Heagle A.B., Frank J. Studies of elongation factor G-dependent tRNA translocation by three-dimensional cryoelectron microscopy. Garret R.A., Douthwaite S.R., Liljas A., Matheson T., Moore P.B., Noller H.F. The Ribosome. Structure, Function, Antibiotics and Cellular Interactions:2000;53-62 ASM Press, Washington, D.C. a.
    • (2000) The Ribosome: Structure, Function, Antibiotics and Cellular Interactions , pp. 53-62
    • Agrawal, R.K.1    Heagle, A.B.2    Frank, J.3
  • 4
  • 5
    • 0034637111 scopus 로고    scopus 로고
    • The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution
    • Ban N., Nissen P., Hansen J., Moore P.B., Steitz T.A. 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
  • 6
    • 0029994962 scopus 로고    scopus 로고
    • Truncated elongation factor G lacking the G domain promotes translocation of the 3′ end but not of the anticodon domain of peptidyl-tRNA
    • Borowski C., Rodnina M.V., Wintermeyer W. Truncated elongation factor G lacking the G domain promotes translocation of the 3′ end but not of the anticodon domain of peptidyl-tRNA. Proc. Natl. Acad. Sci. USA. 93:1996;4202-4206.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 4202-4206
    • Borowski, C.1    Rodnina, M.V.2    Wintermeyer, W.3
  • 7
    • 0014422075 scopus 로고
    • Translocation in protein synthesis: A hybrid structure model
    • Bretscher M.S. Translocation in protein synthesis. a hybrid structure model Nature. 218:1968;675-677.
    • (1968) Nature , vol.218 , pp. 675-677
    • Bretscher, M.S.1
  • 8
    • 0027980558 scopus 로고
    • The crystal structure of elongation factor G complexed with GDP, at 2.7 Å resolution
    • Czworkowski J., Wang J., Steitz T.A., Moore P.B. The crystal structure of elongation factor G complexed with GDP, at 2.7 Å resolution. EMBO J. 13:1994;3661-3668.
    • (1994) EMBO J. , vol.13 , pp. 3661-3668
    • Czworkowski, J.1    Wang, J.2    Steitz, T.A.3    Moore, P.B.4
  • 9
    • 0034691576 scopus 로고    scopus 로고
    • A ratchet-like inter-subunit reorganization of the ribosome during translocation
    • Frank J., Agrawal R.K. 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
  • 15
    • 0016430628 scopus 로고
    • Identification of a ribosomal protein necessary for thiostrepton binding to Escherichia coli ribosomes
    • Highland J.H., Howard G.A., Ochsner E., Hasenbank R., Gordon J., Stoffler G. Identification of a ribosomal protein necessary for thiostrepton binding to Escherichia coli ribosomes. J. Biol. Chem. 250:1975;1141-1145.
    • (1975) J. Biol. Chem. , vol.250 , pp. 1141-1145
    • Highland, J.H.1    Howard, G.A.2    Ochsner, E.3    Hasenbank, R.4    Gordon, J.5    Stoffler, G.6
  • 17
    • 0014939865 scopus 로고
    • Release of transfer ribonucleic acid from ribosomes. A G factor and guanosine triphosphate-dependent reaction
    • Ishitsuka H., Kuriki Y., Kaji A. Release of transfer ribonucleic acid from ribosomes. A G factor and guanosine triphosphate-dependent reaction. J. Biol. Chem. 245:1970;3346-3351.
    • (1970) J. Biol. Chem. , vol.245 , pp. 3346-3351
    • Ishitsuka, H.1    Kuriki, Y.2    Kaji, A.3
  • 18
    • 84889120137 scopus 로고
    • Improved methods for binding protein models in electron density maps and the location of errors in these models
    • Jones T.A., Zhou J.Y., Cowan S.W., Kjeldgaard M. Improved methods for binding protein models in electron density maps and the location of errors in these models. Acta Crystallogr. A. 47:1991;110-119.
    • (1991) Acta Crystallogr. A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zhou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 19
    • 0032526979 scopus 로고    scopus 로고
    • EF-G catalyzed translocation of anticodon stem-loop analogs of transfer RNA in the ribosome
    • Joseph S., Noller H. EF-G catalyzed translocation of anticodon stem-loop analogs of transfer RNA in the ribosome. EMBO J. 17:1998;3478-3483.
    • (1998) EMBO J. , vol.17 , pp. 3478-3483
    • Joseph, S.1    Noller, H.2
  • 20
    • 0033063428 scopus 로고    scopus 로고
    • Novel roles for classical factors at the interface between translation termination and initiation
    • Karimi R., Pavlov M.Y., Buckingham R.H., Ehrenberg M. Novel roles for classical factors at the interface between translation termination and initiation. Mol. Cell. 3:1999;601-609.
    • (1999) Mol. Cell , vol.3 , pp. 601-609
    • Karimi, R.1    Pavlov, M.Y.2    Buckingham, R.H.3    Ehrenberg, M.4
  • 21
    • 0037020031 scopus 로고    scopus 로고
    • Orientation of ribosome recycling factor in the ribosome from directed hydroxyl radical probing
    • Lancaster L., Kiel M.C., Kaji A., Noller H.F. Orientation of ribosome recycling factor in the ribosome from directed hydroxyl radical probing. Cell. 111:2002;129-140.
    • (2002) Cell , vol.111 , pp. 129-140
    • Lancaster, L.1    Kiel, M.C.2    Kaji, A.3    Noller, H.F.4
  • 23
    • 0024841098 scopus 로고
    • Binding of the 3′ terminus of tRNA to 23S rRNA in the ribosomal exit site actively promotes translocation
    • Lill R., Robertson J.M., Wintermeyer W. Binding of the 3′ terminus of tRNA to 23S rRNA in the ribosomal exit site actively promotes translocation. EMBO J. 8:1989;3933-3938.
    • (1989) EMBO J. , vol.8 , pp. 3933-3938
    • Lill, R.1    Robertson, J.M.2    Wintermeyer, W.3
  • 24
    • 0030806152 scopus 로고    scopus 로고
    • A conformational switch in Escherichia coli 16S ribosomal RNA during decoding of messenger RNA
    • Lodmell J.S., Dahlberg A.E. A conformational switch in Escherichia coli 16S ribosomal RNA during decoding of messenger RNA. Science. 277:1997;1262-1267.
    • (1997) Science , vol.277 , pp. 1262-1267
    • Lodmell, J.S.1    Dahlberg, A.E.2
  • 25
    • 0036549804 scopus 로고    scopus 로고
    • Functions and interplay of the tRNA-binding sites of the ribosome
    • Marquez V., Wilson D.N., Nierhaus K.H. Functions and interplay of the tRNA-binding sites of the ribosome. Biochem. Soc. Trans. 30:2002;133-140.
    • (2002) Biochem. Soc. Trans. , vol.30 , pp. 133-140
    • Marquez, V.1    Wilson, D.N.2    Nierhaus, K.H.3
  • 26
    • 0024458904 scopus 로고
    • Intermediate states in the movement of transfer RNA in the ribosome
    • Moazed D., Noller H.F. 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
  • 28
    • 0033638447 scopus 로고    scopus 로고
    • Conformational restricted elongation factor G retains GTPase activity but is inactive in translocation on the ribosome
    • Peske F., Matassova N.B., Savelsbergh A., Rodnina M.V., Wintermeyer W. Conformational 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
  • 29
    • 0037154986 scopus 로고    scopus 로고
    • Ribosome structure and the mechanism of translocation
    • Ramakrishnan V. Ribosome structure and the mechanism of translocation. Cell. 108:2002;557-572.
    • (2002) Cell , vol.108 , pp. 557-572
    • Ramakrishnan, V.1
  • 31
    • 0031028688 scopus 로고    scopus 로고
    • Hydrolysis of GTP by elongation factor G drives tRNA movement on the ribosome
    • Rodnina M.V., Savelsberg A., Katunin V.I., Wintermeyer W. 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    Savelsberg, A.2    Katunin, V.I.3    Wintermeyer, W.4
  • 33
    • 0033966203 scopus 로고    scopus 로고
    • Stimulation of the GTPase activity of translation elongation factor G by ribosomal protein L7/L12
    • Savelsbergh A., Mohr D., Wilden D., Wintermeyer W., Rodnina M.V. Stimulation of the GTPase activity of translation elongation factor G by ribosomal protein L7/L12. J. Biol. Chem. 275:2000;890-894.
    • (2000) J. Biol. Chem. , vol.275 , pp. 890-894
    • Savelsbergh, A.1    Mohr, D.2    Wilden, D.3    Wintermeyer, W.4    Rodnina, M.V.5
  • 37
    • 0034603196 scopus 로고    scopus 로고
    • Large-scale movement of elongation factor G and extensive conformational change of the ribosome during translocation
    • Stark H., Rodnina M.V., Wieden H., van Heel M., Wintermeyer W. Large-scale movement of elongation factor G and extensive conformational change of the ribosome during translocation. Cell. 100:2000;301-309.
    • (2000) Cell , vol.100 , pp. 301-309
    • Stark, H.1    Rodnina, M.V.2    Wieden, H.3    Van Heel, M.4    Wintermeyer, W.5
  • 38
    • 0036829080 scopus 로고    scopus 로고
    • Ribosome interactions of aminoacyl-tRNA and elongation factor Tu in the codon-recognition complex
    • Stark H., Rodnina M.V., Wieden H., Zemlin F., Wintermeyer W., van Heel M. Ribosome interactions of aminoacyl-tRNA and elongation factor Tu in the codon-recognition complex. Nat. Struct. Biol. 9:2002;849-854.
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 849-854
    • Stark, H.1    Rodnina, M.V.2    Wieden, H.3    Zemlin, F.4    Wintermeyer, W.5    Van Heel, M.6
  • 39
    • 0019257050 scopus 로고
    • Functional studies on ribosomes lacking protein L1 from mutant E. coli
    • Subramanian A.R., Dabbs E.R. Functional studies on ribosomes lacking protein L1 from mutant E. coli. Eur. J. Biochem. 112:1980;425-430.
    • (1980) Eur. J. Biochem. , vol.112 , pp. 425-430
    • Subramanian, A.R.1    Dabbs, E.R.2
  • 40
    • 0002445013 scopus 로고
    • The puromycin reaction and its relation to protein synthesis
    • Traut R.R., Monro R.E. The puromycin reaction and its relation to protein synthesis. J. Mol. Biol. 10:1964;63-72.
    • (1964) J. Mol. Biol. , vol.10 , pp. 63-72
    • Traut, R.R.1    Monro, R.E.2
  • 42
  • 46
    • 0038300651 scopus 로고    scopus 로고
    • Peptidyl-tRNA regulates the GTPase activity of translation factors
    • this issue
    • Zavialov A.V., Ehrenberg M. Peptidyl-tRNA regulates the GTPase activity of translation factors. Cell. 114:2003;113-122., this issue.
    • (2003) Cell , vol.114 , pp. 113-122
    • Zavialov, A.V.1    Ehrenberg, M.2
  • 47
    • 0035812714 scopus 로고    scopus 로고
    • A posttermination ribosomal complex is the guanine exchange factor for peptide release factor RF3
    • Zavialov A.V., Buckingham R.H., Ehrenberg M. A posttermination ribosomal complex is the guanine exchange factor for peptide release factor RF3. Cell. 107:2001;115-124.
    • (2001) Cell , vol.107 , pp. 115-124
    • Zavialov, A.V.1    Buckingham, R.H.2    Ehrenberg, M.3
  • 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
    • Zavialov A.V., Mora L., Buckingham R.H., Ehrenberg M. 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.