메뉴 건너뛰기




Volumn 324, Issue 4, 2002, Pages 611-623

EFG-independent translocation of the mRNA:tRNA complex is promoted by modification of the ribosome with thiol-specific reagents

Author keywords

Antibiotic; EFG; Ribosome; Thiol modification; Translocation

Indexed keywords

4 CHLOROMERCURIBENZOIC ACID; ANTIBIOTIC AGENT; ELONGATION FACTOR G; MESSENGER RNA; NUCLEOTIDE; PROTEIN SUBUNIT; RIBOSOME PROTEIN; TRANSFER RNA;

EID: 0036926943     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(02)01196-8     Document Type: Article
Times cited : (47)

References (33)
  • 2
    • 0022147039 scopus 로고
    • Constraints on the accuracy of messenger RNA movement
    • Kurland, C. G. & Ehrenberg, M. (1985). Constraints on the accuracy of messenger RNA movement. Q. Rev. Biophys. 18, 423-450.
    • (1985) Q. Rev. Biophys. , vol.18 , pp. 423-450
    • Kurland, C.G.1    Ehrenberg, M.2
  • 3
    • 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. (1997). Hydrolysis of GTP by elongation factor G drives tRNA movement on the ribosome [see comments]. 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
  • 5
    • 0034691576 scopus 로고    scopus 로고
    • A ratchet-like inter-subunit reorganization of the ribosome during translocation
    • Frank, J. & Agrawal, R. K. (2000). A ratchet-like inter-subunit reorganization of the ribosome during translocation. Nature, 406, 318-322.
    • (2000) Nature , vol.406 , pp. 318-322
    • Frank, J.1    Agrawal, R.K.2
  • 6
    • 0032982866 scopus 로고    scopus 로고
    • EF-G-dependent GTP hydrolysis induces translocation accompanied by large conformational changes in the 70 S ribosome
    • Agrawal, R. K., Heagle, A. B., Penczek, P., Grassucci, R. A. & Frank, J. (1999). EF-G-dependent GTP hydrolysis induces translocation accompanied by large conformational changes in the 70 S ribosome. Nature Struct. Biol. 6, 643-647.
    • (1999) Nature 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
  • 7
    • 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. (2000). Large-scale movement of elongation factor G and extensive conformational change of the ribosome during translocation. Cell, 100, 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
  • 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. (1994). The crystal structure of elongation factor G complexed with GDP, at 2.7 Å resolution. EMBO J. 13, 3661-3668.
    • (1994) EMBO J. , vol.13 , pp. 3661-3668
    • Czworkowski, J.1    Wang, J.2    Steitz, T.A.3    Moore, P.B.4
  • 10
    • 0035394944 scopus 로고    scopus 로고
    • Making molecules into motors
    • Astumian, R. D. (2001). Making molecules into motors. Sci. Am. 285, 56-64.
    • (2001) Sci. Am. , vol.285 , pp. 56-64
    • Astumian, R.D.1
  • 11
    • 0016008661 scopus 로고
    • Assay for nonenzymatic and enzymatic translocation with Escherichia coli ribosomes
    • Pestka, S. (1974). Assay for nonenzymatic and enzymatic translocation with Escherichia coli ribosomes. Methods Enzymol. 30, 462-470.
    • (1974) Methods Enzymol. , vol.30 , pp. 462-470
    • Pestka, S.1
  • 12
    • 84886634813 scopus 로고
    • Factor-free ("non-enzymic") and factor-dependent systems of translation of polyuridylic acid by Escherichia coli ribosomes
    • Gavrilova, L. P., Kostiashkina, O. E., Koteliansky, V. E., Rutkevitch, N. M. & Spirin, A. S. (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
  • 13
    • 0001420054 scopus 로고
    • Stimulation of "non-enzymic" translocation in ribosomes by p-chloromercuribenzoate
    • Gavrilova, L. P. & Spirin, A. S. (1971). Stimulation of "non-enzymic" translocation in ribosomes by p-chloromercuribenzoate. FEBS Letters, 17, 324-326.
    • (1971) FEBS Letters , vol.17 , pp. 324-326
    • Gavrilova, L.P.1    Spirin, A.S.2
  • 15
    • 0036671344 scopus 로고    scopus 로고
    • Important contribution to catalysis of peptide bond formation by a single ionizing group within the ribosome
    • Katunin, V. I., Muth, G. W., Strobel, S. A., Wintermeyer, W. & Rodnina, M. V. (2002). Important contribution to catalysis of peptide bond formation by a single ionizing group within the ribosome. Mol. Cell, 10, 1-20.
    • (2002) Mol. Cell , vol.10 , pp. 1-20
    • Katunin, V.I.1    Muth, G.W.2    Strobel, S.A.3    Wintermeyer, W.4    Rodnina, M.V.5
  • 17
    • 0024458904 scopus 로고
    • Intermediate states in the movement of transfer RNA in the ribosome
    • Moazed, D. & Noller, H. F. (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
  • 18
    • 0026548529 scopus 로고
    • Puromycin reaction for the A site-bound peptidyl-tRNA
    • Semenkov, Y., Shapkina, T., Makhno, V. & Kirillov, S. (1992). Puromycin reaction for the A site-bound peptidyl-tRNA. FEBS Letters, 296, 207-210.
    • (1992) FEBS Letters , vol.296 , pp. 207-210
    • Semenkov, Y.1    Shapkina, T.2    Makhno, V.3    Kirillov, S.4
  • 19
    • 0033762347 scopus 로고    scopus 로고
    • Energetic contribution of tRNA hybrid state formation to translocation catalysis on the ribosome
    • Semenkov, Y. P., Rodnina, M. V. & Wintermeyer, W. (2000). Energetic contribution of tRNA hybrid state formation to translocation catalysis on the ribosome. Nature Struct. Biol. 7, 1027-1031.
    • (2000) Nature Struct. Biol. , vol.7 , pp. 1027-1031
    • Semenkov, Y.P.1    Rodnina, M.V.2    Wintermeyer, W.3
  • 20
    • 0016688822 scopus 로고
    • Stimulation of polypeptide polymerization by blocking of free sulphydryl groups in Escherichia coli ribosomal proteins
    • Cronenberger, J. H. & Erdmann, V. A. (1975). Stimulation of polypeptide polymerization by blocking of free sulphydryl groups in Escherichia coli ribosomal proteins. J. Mol. Biol. 95, 125-137.
    • (1975) J. Mol. Biol. , vol.95 , pp. 125-137
    • Cronenberger, J.H.1    Erdmann, V.A.2
  • 21
    • 0013814892 scopus 로고
    • Studies on polynucleotides, XLIX. Stimulation of the binding of aminoacyl-sRNA's to ribosomes by ribotrinucleotides and a survey of codon assignments for 20 amino acids
    • Soll, D., Ohtsuka, E., Jones, D. S., Lohrmann, R., Hayatsu, H., Nishimura, S. & Khorana, H. G. (1965). Studies on polynucleotides, XLIX. Stimulation of the binding of aminoacyl-sRNA's to ribosomes by ribotrinucleotides and a survey of codon assignments for 20 amino acids. Proc. Natl. Acad. Sci. USA, 54, 1378-1385.
    • (1965) Proc. Natl. Acad. Sci. USA , vol.54 , pp. 1378-1385
    • Soll, D.1    Ohtsuka, E.2    Jones, D.S.3    Lohrmann, R.4    Hayatsu, H.5    Nishimura, S.6    Khorana, H.G.7
  • 22
    • 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. (1996). 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, 4202-4206.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 4202-4206
    • Borowski, C.1    Rodnina, M.V.2    Wintermeyer, W.3
  • 23
    • 0033629418 scopus 로고    scopus 로고
    • Translational frameshifting: Implications for the mechanism of translational frame maintenance
    • Farabaugh, P. J. (2000). Translational frameshifting: Implications for the mechanism of translational frame maintenance. Prog. Nucl. Acid Res. Mol. Biol. 64, 131-170.
    • (2000) Prog. Nucl. Acid Res. Mol. Biol. , vol.64 , pp. 131-170
    • Farabaugh, P.J.1
  • 24
    • 0036282055 scopus 로고    scopus 로고
    • Accurate translocation of mRNA by the ribosome requires a peptidyl group or its analog on the tRNA moving into the 30 S P site
    • Fredrick, K. & Noller, H. F. (2002). Accurate translocation of mRNA by the ribosome requires a peptidyl group or its analog on the tRNA moving into the 30 S P site. Mol. Cell, 9, 1125-1131.
    • (2002) Mol. Cell , vol.9 , pp. 1125-1131
    • Fredrick, K.1    Noller, H.F.2
  • 26
    • 0034903851 scopus 로고    scopus 로고
    • Translation: In retrospect and prospect
    • Woese, C. R. (2001). Translation: In retrospect and prospect. RNA, 7, 1055-1067.
    • (2001) RNA , vol.7 , pp. 1055-1067
    • Woese, C.R.1
  • 27
    • 0017841059 scopus 로고
    • The role of guanine nucleotides in protein biosynthesis
    • Kurland, C. G. (1978). The role of guanine nucleotides in protein biosynthesis. Biophys. J. 22, 373-392.
    • (1978) Biophys. J. , vol.22 , pp. 373-392
    • Kurland, C.G.1
  • 28
    • 0022916242 scopus 로고
    • Transfer RNA shields specific nucleotides in 16 S ribosomal RNA from attack by chemical probes
    • Moazed, D. & Noller, H. F. (1986). Transfer RNA shields specific nucleotides in 16 S ribosomal RNA from attack by chemical probes. Cell, 47, 985-994.
    • (1986) Cell , vol.47 , pp. 985-994
    • Moazed, D.1    Noller, H.F.2
  • 29
    • 0033534197 scopus 로고    scopus 로고
    • Nucleotides in 16 S rRNA protected by the association of 30 S and 50 S ribosomal subunits
    • Merryman, C., Moazed, D., McWhirter, J. & Noller, H. F. (1999). Nucleotides in 16 S rRNA protected by the association of 30 S and 50 S ribosomal subunits. J. Mol. Biol. 285, 97-105.
    • (1999) J. Mol. Biol. , vol.285 , pp. 97-105
    • Merryman, C.1    Moazed, D.2    McWhirter, J.3    Noller, H.F.4
  • 30
    • 0024252185 scopus 로고
    • Extension inhibition analysis of translation initiation complexes
    • Hartz, D., McPheeters, D. S., Traut, R. & Gold, L. (1988). Extension inhibition analysis of translation initiation complexes. Methods Enzymol. 164, 419-425.
    • (1988) Methods Enzymol. , vol.164 , pp. 419-425
    • Hartz, D.1    McPheeters, D.S.2    Traut, R.3    Gold, L.4
  • 31
    • 0029873397 scopus 로고    scopus 로고
    • Rate of translation of natural mRNAs in an optimized in vitro system
    • Pavlov, M. Y. & Ehrenberg, M. (1996). Rate of translation of natural mRNAs in an optimized in vitro system. Arch. Biochem. Biophys. 328, 9-16.
    • (1996) Arch. Biochem. Biophys. , vol.328 , pp. 9-16
    • Pavlov, M.Y.1    Ehrenberg, M.2
  • 32
    • 0032498266 scopus 로고    scopus 로고
    • Mapping the position of translational elongation factor EF-G in the ribosome by directed hydroxyl radical probing
    • Wilson, K. S. & Noller, H. F. (1998). Mapping the position of translational elongation factor EF-G in the ribosome by directed hydroxyl radical probing. Cell, 92, 131-139.
    • (1998) Cell , vol.92 , pp. 131-139
    • Wilson, K.S.1    Noller, H.F.2
  • 33
    • 0019492241 scopus 로고
    • Purification and properties of Escherichia coli translational initiation factors
    • Pawlik, R. T., Littlechild, J., Pon, C. L. & Gualerzi, C. (1981). Purification and properties of Escherichia coli translational initiation factors. Biochem. Int. 2, 421-428.
    • (1981) Biochem. Int. , vol.2 , pp. 421-428
    • Pawlik, R.T.1    Littlechild, J.2    Pon, C.L.3    Gualerzi, C.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.