메뉴 건너뛰기




Volumn 48, Issue 22, 2009, Pages 4699-4706

Interaction of IF2 with the ribosomal GTPase-associated center during 70S initiation complex formation

Author keywords

[No Author keywords available]

Indexed keywords

BACILLUS STEAROTHERMOPHILUS; COMPLEX FORMATIONS; DIPEPTIDE; DYNAMIC LEVELS; E. COLI; ELONGATION FACTOR; GTP HYDROLYSIS; INITIATION FACTORS; N-TERMINAL DOMAINS; RAPID DEVELOPMENT; RELATIVE REACTIVITIES; SENSITIVE PROBE; SIC FORMATION;

EID: 66649100512     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi900222e     Document Type: Article
Times cited : (22)

References (47)
  • 1
    • 0025365804 scopus 로고
    • Initiation of mRNA translation in prokaryotes
    • DOI 10.1021/bi00477a001
    • Gualerzi, C. O., and Pon, C. L. (1990) Initiation of mRNA translation in prokaryotes. Biochemistry 29, 5881-5889. (Pubitemid 20201388)
    • (1990) Biochemistry , vol.29 , Issue.25 , pp. 5881-5889
    • Gualerzi, C.O.1    Pon, C.L.2
  • 2
    • 0035999793 scopus 로고    scopus 로고
    • Structure and function of bacterial initiation factors
    • Boelens, R., and Gualerzi, C. O. (2002) Structure and function of bacterial initiation factors. Curr. Protein Pept. Sci. 3, 107-119.
    • (2002) Curr. Protein Pept. Sci. , vol.3 , pp. 107-119
    • Boelens, R.1    Gualerzi, C.O.2
  • 3
    • 0037154986 scopus 로고    scopus 로고
    • Ribosome structure and the mechanism of translation
    • DOI 10.1016/S0092-8674(02)00619-0
    • Ramakrishnan, V. A. (2002) Ribosome structure and the mechanism of translation. Cell 108, 557-572. (Pubitemid 34260880)
    • (2002) Cell , vol.108 , Issue.4 , pp. 557-572
    • Ramakrishnan, V.1
  • 6
    • 33745633068 scopus 로고    scopus 로고
    • Functional conformations of the L11-ribosomal RNA complex revealed by correlative analysis of cryo-EM and molecular dynamics simulations
    • DOI 10.1261/rna.2294806
    • Li, W., Sengupta, J., Rath, B. K., and Frank, J. (2006) Functional conformations of the L11-ribosomal RNA complex revealed by correlative analysis of cryo-EM and molecular dynamics simulations. RNA 12, 1240-1253. (Pubitemid 43990549)
    • (2006) RNA , vol.12 , Issue.7 , pp. 1240-1253
    • Li, W.1    Sengupta, J.2    Rath, B.K.3    Frank, J.4
  • 8
    • 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., Penczek, P., Grassucci, R. A., and Frank, J. (1999) EF-G-dependent GTP hydrolysis induces translocation accompanied by large conformational changes in the 70S ribosome. Nat. Struct. Biol. 6, 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
  • 9
    • 0035943352 scopus 로고    scopus 로고
    • Localization of L11 protein on the ribosome and elucidation of its involvement in EF-G-dependent translocation
    • Agrawal, R. K., Linde, J., Sengupta, J., Nierhaus, K. H., and Frank, J. (2001) Localization of L11 protein on the ribosome and elucidation of its involvement in EF-G-dependent translocation. J. Mol. Biol. 311, 777-787.
    • (2001) J. Mol. Biol. , vol.311 , pp. 777-787
    • Agrawal, R.K.1    Linde, J.2    Sengupta, J.3    Nierhaus, K.H.4    Frank, J.5
  • 10
    • 0034691576 scopus 로고    scopus 로고
    • A ratchet-like inter-subunit reorganization of the ribosome during translocation
    • DOI 10.1038/35018597
    • Frank, J., and Agrawal, R. K. (2000) A ratchet-like inter-subunit reorganization of the ribosome during translocation. Nature 406, 318-322. (Pubitemid 30604411)
    • (2000) Nature , vol.406 , Issue.6793 , pp. 318-322
    • Frank, J.1    Agrawal, R.K.2
  • 12
    • 20444365142 scopus 로고    scopus 로고
    • The cryo-EM structure of a translation initiation complex from Escherichia coli
    • DOI 10.1016/j.cell.2005.03.023, PII S0092867405002953
    • Allen, G. S., Zavialov, A., Gursky, R., Ehrenberg, M., and Frank, J. (2005) The cryo-EM structure of a translation initiation complex from Escherichia coli. Cell 121, 703-712. (Pubitemid 40797593)
    • (2005) Cell , vol.121 , Issue.5 , pp. 703-712
    • Allen, G.S.1    Zavialov, A.2    Gursky, R.3    Ehrenberg, M.4    Frank, J.5
  • 13
    • 21244465843 scopus 로고    scopus 로고
    • Structural basis for the function of the ribosomal L7/12 stalk in factor binding and GTpase activation
    • DOI 10.1016/j.cell.2005.04.015, PII S0092867405003958
    • Diaconu, M., Kothe, U., Schlünzen, F., Fischer, N., Harms, J. M., Tonevitsky, A. G., Stark, H., Rodnina, M. V., and Wahl, M. C. (2005) Structural basis for the function of the ribosomal L7/12 stalk in factor binding and GTPase activation. Cell 121, 991-1004. (Pubitemid 40884392)
    • (2005) Cell , vol.121 , Issue.7 , pp. 991-1004
    • Diaconu, M.1    Kothe, U.2    Schlunzen, F.3    Fischer, N.4    Harms, J.M.5    Tonevitsky, A.G.6    Stark, H.7    Rodnina, M.V.8    Wahl, M.C.9
  • 15
    • 33644542727 scopus 로고    scopus 로고
    • EF-G-Dependent GTPase on the ribosome. Conformational change and fusidic acid inhibition
    • Seo, H., Abedin, S., Kamp, D., Wilson, D. N., Nierhaus, K. H., and Cooperman, B. S. (2006) EF-G-Dependent GTPase on the ribosome. Conformational change and fusidic acid inhibition. Biochemistry 45, 2504-2514.
    • (2006) Biochemistry , vol.45 , pp. 2504-2514
    • Seo, H.1    Abedin, S.2    Kamp, D.3    Wilson, D.N.4    Nierhaus, K.H.5    Cooperman, B.S.6
  • 17
    • 0029913289 scopus 로고    scopus 로고
    • Late events in translation initiation. Adjustment of fMet-tRNA in the ribosomal P-site
    • La Teana, A., Pon, C. L., and Gualerzi, C. O. (1996) Late events in translation initiation. Adjustment of fMet-tRNA in the ribosomal P-site. J. Mol. Biol. 256, 667-675.
    • (1996) J. Mol. Biol. , vol.256 , pp. 667-675
    • La Teana, A.1    Pon, C.L.2    Gualerzi, C.O.3
  • 18
    • 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., and RajBhandary, U. L. (1997) 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, 1891-1895.
    • (1997) J. Biol. Chem. , vol.272 , pp. 1891-1895
    • Wu, X.Q.1    RajBhandary, U.L.2
  • 19
    • 0022798984 scopus 로고
    • Molecular cloning and sequence of the Bacillus stearothermophilus translational initiation factor IF2 gene
    • Brombach, M., Gualerzi, C. O., Nakamura, Y., and Pon, C. L. (1986) Molecular cloning and sequence of the Bacillus stearothermophilus translational initiation factor IF2 gene. Mol. Gen. Genet. 205, 97-102.
    • (1986) Mol. Gen. Genet. , vol.205 , pp. 97-102
    • Brombach, M.1    Gualerzi, C.O.2    Nakamura, Y.3    Pon, C.L.4
  • 20
    • 34748843156 scopus 로고    scopus 로고
    • A quantitative kinetic scheme for 70 S translation initiation complex formation
    • Grigoriadou, C., Marzi, S., Kirillov, S., Gualerzi, C. O., and Cooperman, B. S. (2007) A quantitative kinetic scheme for 70 S translation initiation complex formation. J. Mol. Biol. 373, 562-572.
    • (2007) J. Mol. Biol. , vol.373 , pp. 562-572
    • Grigoriadou, C.1    Marzi, S.2    Kirillov, S.3    Gualerzi, C.O.4    Cooperman, B.S.5
  • 21
    • 0027151981 scopus 로고
    • Translation of mRNAs with degenerate initiation triplet AUU displays high initiation factor 2 dependence and is subject to initiation factor 3 repression
    • La Teana, A., Pon, C. L., and Gualerzi, C. O. (1993) Translation of mRNAs with degenerate initiation triplet AUU displays high initiation factor 2 dependence and is subject to initiation factor 3 repression. Proc. Natl. Acad. Sci. U.S.A. 90, 4161-4165.
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 4161-4165
    • La Teana, A.1    Pon, C.L.2    Gualerzi, C.O.3
  • 23
    • 33745044746 scopus 로고    scopus 로고
    • Rapid ribosomal translocation depends on the conserved 18-55 base pair in P-site transfer RNA
    • Pan, D., Kirillov, S., Zhang, C. M., Hou, Y. M., and Cooperman, B. S. (2006) Rapid ribosomal translocation depends on the conserved 18-55 base pair in P-site transfer RNA. Nat. Struct. Mol. Biol. 13, 354-359.
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 354-359
    • Pan, D.1    Kirillov, S.2    Zhang, C.M.3    Hou, Y.M.4    Cooperman, B.S.5
  • 25
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 26
    • 34648813439 scopus 로고    scopus 로고
    • Single-molecule structural dynamics of EF-G-ribosome interaction during translocation
    • DOI 10.1021/bi700657d
    • Wang, Y., Qin, H., Kudaravalli, R. D., Kirillov, S. V., Dempsey, G. T., Pan, D., Cooperman, B. S., and Goldman, Y. E. (2007) Single-molecule structural dynamics of EF-G-ribosome interaction during translocation. Biochemistry 46, 10767-10775. (Pubitemid 47463031)
    • (2007) Biochemistry , vol.46 , Issue.38 , pp. 10767-10775
    • Wang, Y.1    Qin, H.2    Kudaravalli, R.D.3    Kirillov, S.V.4    Dempsey, G.T.5    Pan, D.6    Cooperman, B.S.7    Goldman, Y.E.8
  • 27
    • 34748909381 scopus 로고    scopus 로고
    • The translational fdelity function of IF3 during transition from the 30 S initiation complex to the 70 S initiation complex
    • Grigoriadou, C., Marzi, S., Pan, D., Gualerzi, C. O., and Cooperman, B. S. (2007) The translational fdelity function of IF3 during transition from the 30 S initiation complex to the 70 S initiation complex. J. Mol. Biol. 373, 551-561.
    • (2007) J. Mol. Biol. , vol.373 , pp. 551-561
    • Grigoriadou, C.1    Marzi, S.2    Pan, D.3    Gualerzi, C.O.4    Cooperman, B.S.5
  • 28
    • 0028175534 scopus 로고
    • Purification of fMet-tRNA(fMet) by fast protein liquid chromatography
    • Rodnina, M. V., Semenkov, Y. P., and Wintermeyer, W. (1994) Purification of fMet-tRNA(fMet) by fast protein liquid chromatography. Anal. Biochem. 219, 380-381.
    • (1994) Anal. Biochem. , vol.219 , pp. 380-381
    • Rodnina, M.V.1    Semenkov, Y.P.2    Wintermeyer, W.3
  • 29
    • 33847024820 scopus 로고    scopus 로고
    • Kinetically Competent Intermediates in the Translocation Step of Protein Synthesis
    • DOI 10.1016/j.molcel.2007.01.014, PII S1097276507000366
    • Pan, D., Kirillov, S. V., and Cooperman, B. S. (2007) Kinetically competent intermediates in the translocation step of protein synthesis. Mol. Cell 25, 519-529. (Pubitemid 46274443)
    • (2007) Molecular Cell , vol.25 , Issue.4 , pp. 519-529
    • Pan, D.1    Kirillov, S.V.2    Cooperman, B.S.3
  • 32
    • 0028884014 scopus 로고
    • Fluorescence resonance energy transfer spectroscopy is a reliable "ruler" for measuring structural changes in proteins. Dispelling the problem of the unknown orientation factor
    • dos Remedios, C. G., and Moens, P. D. (1995) Fluorescence resonance energy transfer spectroscopy is a reliable "ruler" for measuring structural changes in proteins. Dispelling the problem of the unknown orientation factor. J. Struct. Biol. 115, 175-185.
    • (1995) J. Struct. Biol. , vol.115 , pp. 175-185
    • Dos Remedios, C.G.1    Moens, P.D.2
  • 34
    • 0041923728 scopus 로고    scopus 로고
    • The ATP-waiting conformation of rotating F1-ATPase revealed by single-pair fluorescence resonance energy transfer
    • Yasuda, R., Masaike, T., Adachi, K., Noji, H., Itoh, H., and Kinosita, K.Jr. (2003) The ATP-waiting conformation of rotating F1-ATPase revealed by single-pair fluorescence resonance energy transfer. Proc. Natl. Acad. Sci. U.S.A. 100, 9314-9318.
    • (2003) Proc. Natl. Acad. Sci. U.S.A. , vol.100 , pp. 9314-9318
    • Yasuda, R.1    Masaike, T.2    Adachi, K.3    Noji, H.4    Itoh, H.5    Kinosita Jr., K.6
  • 37
    • 0017105960 scopus 로고
    • The involvement of protein L11 in the joining of the 30-S initiation complex to the 50-S subunit
    • Naaktgeboren, N., Schrier, P.,Möller, W., and Voorma, H. O. (1976) The involvement of protein L11 in the joining of the 30-S initiation complex to the 50-S subunit. Eur. J. Biochem. 62, 117-123.
    • (1976) Eur. J. Biochem. , vol.62 , pp. 117-123
    • Naaktgeboren, N.1    Schrier, P.2    Möller, W.3    Voorma, H.O.4
  • 38
    • 0024327216 scopus 로고
    • Subunit association defects in Escherichia coli ribosome mutants lacking proteins S20 and L11
    • Götz, F., Fleischer, C., Pon, C. L., and Gualerzi, C. O. (1989) Subunit association defects in Escherichia coli ribosome mutants lacking proteins S20 and L11. Eur. J. Biochem. 183, 19-24.
    • (1989) Eur. J. Biochem. , vol.183 , pp. 19-24
    • Götz, F.1    Fleischer, C.2    Pon, C.L.3    Gualerzi, C.O.4
  • 39
  • 40
    • 0017258710 scopus 로고
    • Reconstitution of Bacillus stearothermophilus 50 S ribosomal subunits from purified molecular components
    • Cohlberg, J. A., and Nomura, M. (1976) Reconstitution of Bacillus stearothermophilus 50 S ribosomal subunits from purified molecular components. J. Biol. Chem. 251, 209-221.
    • (1976) J. Biol. Chem. , vol.251 , pp. 209-221
    • Cohlberg, J.A.1    Nomura, M.2
  • 41
    • 2342547059 scopus 로고    scopus 로고
    • Ribosome formation from subunits studied by stopped-flow and Rayleigh light-scattering
    • Antoun, A., Pavlov, M. Y., Andersson, K., Tenson, T., and Ehrenberg, M. (2004) Ribosome formation from subunits studied by stopped-flow and Rayleigh light-scattering. Biol. Proced. Online 6, 35-54.
    • (2004) Biol. Proced. Online , vol.6 , pp. 35-54
    • Antoun, A.1    Pavlov, M.Y.2    Andersson, K.3    Tenson, T.4    Ehrenberg, M.5
  • 42
    • 33745763700 scopus 로고    scopus 로고
    • How initiation factors tune the rate of initiation of protein synthesis in bacteria
    • DOI 10.1038/sj.emboj.7601140, PII 7601140
    • Antoun, A., Pavlov, M. Y., Lovmar, M., and Ehrenberg, M. (2006) How initiation factors tune the rate of initiation of protein synthesis in bacteria. EMBO J. 25, 2539-2550. (Pubitemid 44012236)
    • (2006) EMBO Journal , vol.25 , Issue.11 , pp. 2539-2550
    • Antoun, A.1    Pavlov, M.Y.2    Lovmar, M.3    Ehrenberg, M.4
  • 43
    • 44949260971 scopus 로고    scopus 로고
    • Kinetic checkpoint at a late step in translation initiation
    • Milon, P., Konevega, A. L., Gualerzi, C. O., and Rodnina, M. V. (2008) Kinetic checkpoint at a late step in translation initiation. Mol. Cell 30, 712-720.
    • (2008) Mol. Cell , vol.30 , pp. 712-720
    • Milon, P.1    Konevega, A.L.2    Gualerzi, C.O.3    Rodnina, M.V.4
  • 45
    • 44449125068 scopus 로고    scopus 로고
    • Spontaneous intersubunit rotation in single ribosomes
    • Cornish, P. V., Ermolenko, D. N., Noller, H. F., and 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
  • 46
    • 0031028688 scopus 로고    scopus 로고
    • Hydrolysis of GTP by elongation factor G drives tRNA movement on the ribosome
    • DOI 10.1038/385037a0
    • Rodnina, M. V., Savelsbergh, A., Katunin, V. I., and Wintermeyer, W. (1997) Hydrolysis of GTP by elongation factor G drives tRNA movement on the ribosome. Nature 385, 37-41. (Pubitemid 27024544)
    • (1997) Nature , vol.385 , Issue.6611 , pp. 37-41
    • Rodnina, M.V.1    Savelsbergh, A.2    Katunin, V.I.3    Wintermeyer, W.4
  • 47
    • 0038433302 scopus 로고    scopus 로고
    • An Elongation Factor G-Induced Ribosome Rearrangement Precedes tRNA-mRNA Translocation
    • DOI 10.1016/S1097-2765(03)00230-2
    • Savelsbergh, A., Katunin, V. I., Mohr, D., Peske, F., Rodnina, M. V., and Wintermeyer, W. (2003) An elongation factor G-induced ribosome rearrangement precedes tRNA-mRNA translocation. Mol. Cell 11, 1517-1523. (Pubitemid 36776538)
    • (2003) Molecular Cell , vol.11 , Issue.6 , pp. 1517-1523
    • Savelsbergh, A.1    Katunin, V.I.2    Mohr, D.3    Peske, F.4    Rodnina, M.V.5    Wintermeyer, W.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.