메뉴 건너뛰기




Volumn 7, Issue 5, 2014, Pages 1534-1546

Sequence-dependent elongation dynamics on macrolide-bound ribosomes

Author keywords

[No Author keywords available]

Indexed keywords

ERMCL PROTEIN; ERYTHROMYCIN; GUANOSINE TRIPHOSPHATE; HISTONE LIKE NUCLEOID STRUCTURING PROTEIN; MESSENGER RNA; RIBOSOME PROTEIN; TRANSFER RNA; UNCLASSIFIED DRUG; ANTIINFECTIVE AGENT; METHYLTRANSFERASE; PROTEIN BINDING; PROTEIN SYNTHESIS INHIBITOR; RRNA (ADENOSINE-O-2'-)METHYLTRANSFERASE; STOP CODON; MACROLIDE; PEPTIDE; PEPTIDE ERMCL; PEPTIDE H NS;

EID: 84902302739     PISSN: None     EISSN: 22111247     Source Type: Journal    
DOI: 10.1016/j.celrep.2014.04.034     Document Type: Article
Times cited : (30)

References (34)
  • 1
    • 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
  • 3
    • 78049250815 scopus 로고    scopus 로고
    • Revisiting the structures of several antibiotics bound to the bacterial ribosome
    • Bulkley D., Innis C.A., Blaha G., Steitz T.A. Revisiting the structures of several antibiotics bound to the bacterial ribosome. Proc. Natl. Acad. Sci. USA 2010, 107:17158-17163.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 17158-17163
    • Bulkley, D.1    Innis, C.A.2    Blaha, G.3    Steitz, T.A.4
  • 4
    • 84859334880 scopus 로고    scopus 로고
    • Nonfluorescent quenchers to correlate single-molecule conformational and compositional dynamics
    • Chen J., Tsai A., Petrov A., Puglisi J.D. Nonfluorescent quenchers to correlate single-molecule conformational and compositional dynamics. J.Am. Chem. Soc. 2012, 134:5734-5737.
    • (2012) J.Am. Chem. Soc. , vol.134 , pp. 5734-5737
    • Chen, J.1    Tsai, A.2    Petrov, A.3    Puglisi, J.D.4
  • 5
    • 84878909556 scopus 로고    scopus 로고
    • Coordinated conformational and compositional dynamics drive ribosome translocation
    • Chen J., Petrov A., Tsai A., O'Leary S.E., Puglisi J.D. Coordinated conformational and compositional dynamics drive ribosome translocation. Nat. Struct. Mol. Biol. 2013, 20:718-727.
    • (2013) Nat. Struct. Mol. Biol. , vol.20 , pp. 718-727
    • Chen, J.1    Petrov, A.2    Tsai, A.3    O'Leary, S.E.4    Puglisi, J.D.5
  • 7
    • 0030564828 scopus 로고    scopus 로고
    • Co-variation of tRNA abundance and codon usage in Escherichia coli at different growth rates
    • Dong H., Nilsson L., Kurland C.G. Co-variation of tRNA abundance and codon usage in Escherichia coli at different growth rates. J.Mol. Biol. 1996, 260:649-663.
    • (1996) J.Mol. Biol. , vol.260 , pp. 649-663
    • Dong, H.1    Nilsson, L.2    Kurland, C.G.3
  • 9
    • 78049302075 scopus 로고    scopus 로고
    • Structures of the Escherichia coli ribosome with antibiotics bound near the peptidyl transferase center explain spectra of drug action
    • Dunkle J.A., Xiong L., Mankin A.S., Cate J.H. Structures of the Escherichia coli ribosome with antibiotics bound near the peptidyl transferase center explain spectra of drug action. Proc. Natl. Acad. Sci. USA 2010, 107:17152-17157.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 17152-17157
    • Dunkle, J.A.1    Xiong, L.2    Mankin, A.S.3    Cate, J.H.4
  • 10
    • 61649098586 scopus 로고    scopus 로고
    • Statics of the ribosomal exit tunnel: implications for cotranslational peptide folding, elongation regulation, and antibiotics binding
    • Fulle S., Gohlke H. Statics of the ribosomal exit tunnel: implications for cotranslational peptide folding, elongation regulation, and antibiotics binding. J.Mol. Biol. 2009, 387:502-517.
    • (2009) J.Mol. Biol. , vol.387 , pp. 502-517
    • Fulle, S.1    Gohlke, H.2
  • 11
    • 44449089912 scopus 로고    scopus 로고
    • The kinetics of ribosomal peptidyl transfer revisited
    • Johansson M., Bouakaz E., Lovmar M., Ehrenberg M. The kinetics of ribosomal peptidyl transfer revisited. Mol. Cell 2008, 30:589-598.
    • (2008) Mol. Cell , vol.30 , pp. 589-598
    • Johansson, M.1    Bouakaz, E.2    Lovmar, M.3    Ehrenberg, M.4
  • 12
    • 84862963791 scopus 로고    scopus 로고
    • Genetic code translation displays a linear trade-off between efficiency and accuracy of tRNA selection
    • Johansson M., Zhang J., Ehrenberg M. Genetic code translation displays a linear trade-off between efficiency and accuracy of tRNA selection. Proc. Natl. Acad. Sci. USA 2012, 109:131-136.
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 131-136
    • Johansson, M.1    Zhang, J.2    Ehrenberg, M.3
  • 13
    • 84255195557 scopus 로고    scopus 로고
    • Macrolide antibiotics in the ribosome exit tunnel: species-specific binding and action
    • Kannan K., Mankin A.S. Macrolide antibiotics in the ribosome exit tunnel: species-specific binding and action. Ann. N Y Acad. Sci. 2011, 1241:33-47.
    • (2011) Ann. N Y Acad. Sci. , vol.1241 , pp. 33-47
    • Kannan, K.1    Mankin, A.S.2
  • 14
    • 84868035954 scopus 로고    scopus 로고
    • Selective protein synthesis by ribosomes with a drug-obstructed exit tunnel
    • Kannan K., Vázquez-Laslop N., Mankin A.S. Selective protein synthesis by ribosomes with a drug-obstructed exit tunnel. Cell 2012, 151:508-520.
    • (2012) Cell , vol.151 , pp. 508-520
    • Kannan, K.1    Vázquez-Laslop, N.2    Mankin, A.S.3
  • 16
    • 51649118422 scopus 로고    scopus 로고
    • Folding at the rhythm of the rare codon beat
    • Marin M. Folding at the rhythm of the rare codon beat. Biotechnol. J. 2008, 3:1047-1057.
    • (2008) Biotechnol. J. , vol.3 , pp. 1047-1057
    • Marin, M.1
  • 17
    • 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. USA 2008, 105:15364-15369.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 15364-15369
    • Marshall, R.A.1    Dorywalska, M.2    Puglisi, J.D.3
  • 19
    • 0020322533 scopus 로고
    • Erythromycin, carbomycin, and spiramycin inhibit protein synthesis by stimulating the dissociation of peptidyl-tRNA from ribosomes
    • Menninger J.R., Otto D.P. Erythromycin, carbomycin, and spiramycin inhibit protein synthesis by stimulating the dissociation of peptidyl-tRNA from ribosomes. Antimicrob. Agents Chemother. 1982, 21:811-818.
    • (1982) Antimicrob. Agents Chemother. , vol.21 , pp. 811-818
    • Menninger, J.R.1    Otto, D.P.2
  • 20
    • 0029873397 scopus 로고    scopus 로고
    • Rate of translation of natural mRNAs in an optimized invitro system
    • Pavlov M.Y., Ehrenberg M. Rate of translation of natural mRNAs in an optimized invitro system. Arch. Biochem. Biophys. 1996, 328:9-16.
    • (1996) Arch. Biochem. Biophys. , vol.328 , pp. 9-16
    • Pavlov, M.Y.1    Ehrenberg, M.2
  • 21
    • 79251557798 scopus 로고    scopus 로고
    • Nascent peptide in the ribosome exit tunnel affects functional properties of the A-site of the peptidyl transferase center
    • Ramu H., Vázquez-Laslop N., Klepacki D., Dai Q., Piccirilli J., Micura R., Mankin A.S. Nascent peptide in the ribosome exit tunnel affects functional properties of the A-site of the peptidyl transferase center. Mol. Cell 2011, 41:321-330.
    • (2011) Mol. Cell , vol.41 , pp. 321-330
    • Ramu, H.1    Vázquez-Laslop, N.2    Klepacki, D.3    Dai, Q.4    Piccirilli, J.5    Micura, R.6    Mankin, A.S.7
  • 22
    • 0020316476 scopus 로고
    • Temperature dependence of RNA synthesis parameters in Escherichia coli
    • Ryals J., Little R., Bremer H. Temperature dependence of RNA synthesis parameters in Escherichia coli. J.Bacteriol. 1982, 151:879-887.
    • (1982) J.Bacteriol. , vol.151 , pp. 879-887
    • Ryals, J.1    Little, R.2    Bremer, H.3
  • 24
    • 0034817784 scopus 로고    scopus 로고
    • Short peptides conferring resistance to macrolide antibiotics
    • Tenson T., Mankin A.S. Short peptides conferring resistance to macrolide antibiotics. Peptides 2001, 22:1661-1668.
    • (2001) Peptides , vol.22 , pp. 1661-1668
    • Tenson, T.1    Mankin, A.S.2
  • 25
    • 0038690158 scopus 로고    scopus 로고
    • The mechanism of action of macrolides, lincosamides and streptogramin B reveals the nascent peptide exit path in the ribosome
    • Tenson T., Lovmar M., Ehrenberg M. The mechanism of action of macrolides, lincosamides and streptogramin B reveals the nascent peptide exit path in the ribosome. J.Mol. Biol. 2003, 330:1005-1014.
    • (2003) J.Mol. Biol. , vol.330 , pp. 1005-1014
    • Tenson, T.1    Lovmar, M.2    Ehrenberg, M.3
  • 26
    • 84863986007 scopus 로고    scopus 로고
    • Heterogeneous pathways and timing of factor departure during translation initiation
    • Tsai A., Petrov A., Marshall R.A., Korlach J., Uemura S., Puglisi J.D. Heterogeneous pathways and timing of factor departure during translation initiation. Nature 2012, 487:390-393.
    • (2012) Nature , vol.487 , pp. 390-393
    • Tsai, A.1    Petrov, A.2    Marshall, R.A.3    Korlach, J.4    Uemura, S.5    Puglisi, J.D.6
  • 28
    • 84902327338 scopus 로고    scopus 로고
    • The dynamics of SecM-induced translational stalling
    • this issue
    • Tsai A., Kornberg G., Johansson M., Chen J., Puglisi J.D. The dynamics of SecM-induced translational stalling. Cell Rep. 2014, 7:1521-1533. this issue.
    • (2014) Cell Rep. , vol.7 , pp. 1521-1533
    • Tsai, A.1    Kornberg, G.2    Johansson, M.3    Chen, J.4    Puglisi, J.D.5
  • 29
    • 17444421169 scopus 로고    scopus 로고
    • Structures of MLSBK antibiotics bound to mutated large ribosomal subunits provide a structural explanation for resistance
    • Tu D., Blaha G., Moore P.B., Steitz T.A. Structures of MLSBK antibiotics bound to mutated large ribosomal subunits provide a structural explanation for resistance. Cell 2005, 121:257-270.
    • (2005) Cell , vol.121 , pp. 257-270
    • Tu, D.1    Blaha, G.2    Moore, P.B.3    Steitz, T.A.4
  • 31
    • 43049089746 scopus 로고    scopus 로고
    • Molecular mechanism of drug-dependent ribosome stalling
    • Vazquez-Laslop N., Thum C., Mankin A.S. Molecular mechanism of drug-dependent ribosome stalling. Mol. Cell 2008, 30:190-202.
    • (2008) Mol. Cell , vol.30 , pp. 190-202
    • Vazquez-Laslop, N.1    Thum, C.2    Mankin, A.S.3
  • 32
    • 0028914553 scopus 로고
    • Insights into erythromycin action from studies of its activity as inducer of resistance
    • Weisblum B. Insights into erythromycin action from studies of its activity as inducer of resistance. Antimicrob. Agents Chemother. 1995, 39:797-805.
    • (1995) Antimicrob. Agents Chemother. , vol.39 , pp. 797-805
    • Weisblum, B.1
  • 33
    • 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
  • 34
    • 79953106751 scopus 로고    scopus 로고
    • The ribosomal tunnel as a functional environment for nascent polypeptide folding and translational stalling
    • Wilson D.N., Beckmann R. The ribosomal tunnel as a functional environment for nascent polypeptide folding and translational stalling. Curr. Opin. Struct. Biol. 2011, 21:274-282.
    • (2011) Curr. Opin. Struct. Biol. , vol.21 , pp. 274-282
    • Wilson, D.N.1    Beckmann, R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.