메뉴 건너뛰기




Volumn 114, Issue 1, 2003, Pages 113-122

Peptidyl-tRNA regulates the GTPase activity of translation factors

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; ELONGATION FACTOR G; ELONGATION FACTOR TU; FUSIDIC ACID; GUANINE NUCLEOTIDE BINDING PROTEIN; GUANOSINE TRIPHOSPHATASE; INITIATION FACTOR 2; PEPTIDE RELEASE FACTOR; TRANSFER RNA; UNCLASSIFIED DRUG;

EID: 0038300651     PISSN: 00928674     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0092-8674(03)00478-1     Document Type: Article
Times cited : (122)

References (34)
  • 2
    • 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., 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.2    Wintermeyer, W.3
  • 3
    • 0026026818 scopus 로고
    • The GTPase superfamily: Conserved structure and molecular mechanism
    • Bourne H.R., Sanders D.A., McCormick F. The GTPase superfamily. conserved structure and molecular mechanism Nature. 349:1991;117-127.
    • (1991) Nature , vol.349 , pp. 117-127
    • Bourne, H.R.1    Sanders, D.A.2    McCormick, F.3
  • 4
    • 0014422075 scopus 로고
    • Translocation in protein synthesis: A hybrid structure model
    • Bretscher M. Translocation in protein synthesis. a hybrid structure model Nature. 218:1968;675-677.
    • (1968) Nature , vol.218 , pp. 675-677
    • Bretscher, M.1
  • 5
    • 0015962113 scopus 로고
    • A resolution of conflicting reports concerning the mode of action of fusidic acid
    • Burns U., Cannon M., Cundliffe E. A resolution of conflicting reports concerning the mode of action of fusidic acid. FEBS Lett. 40:1974;219-223.
    • (1974) FEBS Lett. , vol.40 , pp. 219-223
    • Burns, U.1    Cannon, M.2    Cundliffe, E.3
  • 6
    • 0036301166 scopus 로고    scopus 로고
    • Initiation factor IF2, thiostrepton and micrococcin prevent the binding of elongation factor G to the Escherichia coli ribosome
    • Cameron D.M., Thompson J., March P.E., Dahlberg A.E. Initiation factor IF2, thiostrepton and micrococcin prevent the binding of elongation factor G to the Escherichia coli ribosome. J. Mol. Biol. 319:2002;27-35.
    • (2002) J. Mol. Biol. , vol.319 , pp. 27-35
    • Cameron, D.M.1    Thompson, J.2    March, P.E.3    Dahlberg, A.E.4
  • 8
    • 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
  • 11
    • 0016220086 scopus 로고
    • The role of guanosine triphosphate in translocation reaction catalyzed by elongation factor G
    • Inoue-Yokosawa N., Ishikawa C., Kaziro Y. The role of guanosine triphosphate in translocation reaction catalyzed by elongation factor G. J. Biol. Chem. 249:1974;4321-4323.
    • (1974) J. Biol. Chem. , vol.249 , pp. 4321-4323
    • Inoue-Yokosawa, N.1    Ishikawa, C.2    Kaziro, Y.3
  • 12
    • 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
  • 13
    • 0037159243 scopus 로고    scopus 로고
    • Coupling of GTP hydrolysis by elongation factor G to translocation and factor recycling on the ribosome
    • Katunin V.I., Savelsbergh A., Rodnina M.V., Wintermeyer W. Coupling of GTP hydrolysis by elongation factor G to translocation and factor recycling on the ribosome. Biochemistry. 41:2002;12806-12812.
    • (2002) Biochemistry , vol.41 , pp. 12806-12812
    • Katunin, V.I.1    Savelsbergh, A.2    Rodnina, M.V.3    Wintermeyer, W.4
  • 14
    • 0037439231 scopus 로고    scopus 로고
    • Termination of translation: Interplay of mRNA, rRNAs and release factors?
    • Kisselev L., Ehrenberg M., Frolova L. Termination of translation. interplay of mRNA, rRNAs and release factors? EMBO J. 22:2003;175-182.
    • (2003) EMBO J. , vol.22 , pp. 175-182
    • Kisselev, L.1    Ehrenberg, M.2    Frolova, L.3
  • 17
    • 0037020031 scopus 로고    scopus 로고
    • Orientation of ribosome recycling factor in the ribosome from directed hydroxyl radical probing
    • Lancaster L., Kiel M., Kaji A., Noller H. 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.2    Kaji, A.3    Noller, H.4
  • 18
    • 0022494313 scopus 로고
    • Affinities of tRNA binding sites of ribosomes from Escherichia coli
    • Lill R., Robertson J.M., Wintermeyer W. Affinities of tRNA binding sites of ribosomes from Escherichia coli. Biochemistry. 25:1986;3245-3255.
    • (1986) Biochemistry , vol.25 , pp. 3245-3255
    • Lill, R.1    Robertson, J.M.2    Wintermeyer, W.3
  • 19
    • 0036549804 scopus 로고    scopus 로고
    • Functions and interplay of the tRNA-binding sites of the ribosome
    • Marquez V., Wilson D., Nierhaus K. 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.2    Nierhaus, K.3
  • 20
    • 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
  • 21
    • 0037223622 scopus 로고    scopus 로고
    • The essential role of the invariant GGQ motif in the function and stability in vivo of bacterial release factors RF1 and RF2
    • Mora L., Heurgue-Hamard V., Champ S., Ehrenberg M., Kisselev L.L., Buckingham R.H. The essential role of the invariant GGQ motif in the function and stability in vivo of bacterial release factors RF1 and RF2. Mol. Microbiol. 47:2003;267-275.
    • (2003) Mol. Microbiol. , vol.47 , pp. 267-275
    • Mora, L.1    Heurgue-Hamard, V.2    Champ, S.3    Ehrenberg, M.4    Kisselev, L.L.5    Buckingham, R.H.6
  • 23
    • 0030928327 scopus 로고    scopus 로고
    • Fast recycling of Escherichia coli ribosomes requires both ribosome recycling factor (RRF) and release factor RF3
    • Pavlov M.Y., Freistroffer D.V., MacDougall J., Buckingham R.H., Ehrenberg M. Fast recycling of Escherichia coli ribosomes requires both ribosome recycling factor (RRF) and release factor RF3. EMBO J. 16:1997;4134-4141.
    • (1997) EMBO J. , vol.16 , pp. 4134-4141
    • Pavlov, M.Y.1    Freistroffer, D.V.2    MacDougall, J.3    Buckingham, R.H.4    Ehrenberg, M.5
  • 24
    • 0037154986 scopus 로고    scopus 로고
    • Ribosome structure and the mechanism of translation
    • Ramakrishnan V. Ribosome structure and the mechanism of translation. Cell. 108:2002;557-572.
    • (2002) Cell , vol.108 , pp. 557-572
    • Ramakrishnan, V.1
  • 26
    • 0031028688 scopus 로고    scopus 로고
    • Hydrolysis of GTP by elongation factor G drives tRNA movement on the ribosome
    • Rodnina M.V., Savelsbergh 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    Savelsbergh, A.2    Katunin, V.I.3    Wintermeyer, W.4
  • 27
    • 0020337390 scopus 로고
    • Is there proofreading during polypeptide synthesis?
    • Ruusala T., Ehrenberg M., Kurland C.G. Is there proofreading during polypeptide synthesis? EMBO J. 1:1982;741-745.
    • (1982) EMBO J. , vol.1 , pp. 741-745
    • Ruusala, T.1    Ehrenberg, M.2    Kurland, C.G.3
  • 28
    • 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.J., 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.J.3    Van Heel, M.4    Wintermeyer, W.5
  • 29
    • 0004955452 scopus 로고
    • Proofreading of the codon-anticodon interaction on ribosomes
    • Thompson R., Stone P.J. Proofreading of the codon-anticodon interaction on ribosomes. Proc. Natl. Acad. Sci. USA. 74:1977;198-202.
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 198-202
    • Thompson, R.1    Stone, P.J.2
  • 31
    • 0034535129 scopus 로고    scopus 로고
    • Transit of tRNA through the Escherichia coli ribosome. Cross-linking of the 3′ end of tRNA to specific nucleotides of the 23 S ribosomal RNA at the A, P, and E sites
    • Wower J., Kirillov S., Wower I., Guven S., Hixson S., Zimmermann R. Transit of tRNA through the Escherichia coli ribosome. Cross-linking of the 3′ end of tRNA to specific nucleotides of the 23 S ribosomal RNA at the A, P, and E sites. J. Biol. Chem. 275:2000;37887-37894.
    • (2000) J. Biol. Chem. , vol.275 , pp. 37887-37894
    • Wower, J.1    Kirillov, S.2    Wower, I.3    Guven, S.4    Hixson, S.5    Zimmermann, R.6
  • 32
    • 0031026590 scopus 로고    scopus 로고
    • Effect of the amino acid attached to Escherichia coli initiator tRNA on its affinity for the initiation factor IF2 and on the IF2 dependence of its binding to the ribosome
    • Wu X.Q., RajBhandary U.L. Effect of the amino acid attached to Escherichia coli initiator tRNA on its affinity for the initiation factor IF2 and on the IF2 dependence of its binding to the ribosome. J. Biol. Chem. 272:1997;1891-1895.
    • (1997) J. Biol. Chem. , vol.272 , pp. 1891-1895
    • Wu, X.Q.1    RajBhandary, U.L.2
  • 33
    • 0035812714 scopus 로고    scopus 로고
    • A posttermination ribosomal complex is the guanine nucleotide exchange factor for peptide release factor RF3
    • Zavialov A.V., Buckingham R.H., Ehrenberg M. A posttermination ribosomal complex is the guanine nucleotide 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
  • 34
    • 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.