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Volumn , Issue 48, 2010, Pages

Isolation of translating ribosomes containing peptidyl-tRNAs for functional and structural analyses

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EID: 80355125355     PISSN: 1940087X     EISSN: None     Source Type: Journal    
DOI: 10.3791/2498     Document Type: Article
Times cited : (2)

References (20)
  • 1
    • 33644851066 scopus 로고    scopus 로고
    • Changes produced by bound tryptophan in the ribosome peptidyl transferase center in response to tnaC, a nascent leader peptide
    • Cruz-Vera, L. R., Gong, M. & Yanofsky, C. Changes produced by bound tryptophan in the ribosome peptidyl transferase center in response to tnaC, a nascent leader peptide. Proc. Natl. Acad. Sci. U. S. A 103, 3598-603 (2006).
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 3598-3603
    • Cruz-Vera, L.R.1    Gong, M.2    Yanofsky, C.3
  • 2
    • 0035162904 scopus 로고    scopus 로고
    • Binding site of macrolide antibiotics on the ribosome: New resistance mutation identifies a specific interaction of ketolides with rRNA
    • Garza-Ramos, G., Xiong, L., Zhong, P. & Mankin, A. Binding site of macrolide antibiotics on the ribosome: new resistance mutation identifies a specific interaction of ketolides with rRNA. J. Bacteriol 183, 6898-907 (2001).
    • (2001) J. Bacteriol , vol.183 , pp. 6898-6907
    • Garza-Ramos, G.1    Xiong, L.2    Zhong, P.3    Mankin, A.4
  • 3
    • 0038135144 scopus 로고    scopus 로고
    • Macrolide antibiotics: Binding site, mechanism of action, resistance
    • Gaynor, M. & Mankin, A. S. Macrolide antibiotics: binding site, mechanism of action, resistance. Curr. Top. Med. Chem 3, 949-61 (2003).
    • (2003) Curr. Top. Med. Chem , vol.3 , pp. 949-961
    • Gaynor, M.1    Mankin, A.S.2
  • 4
    • 31344478504 scopus 로고    scopus 로고
    • The ribosomal peptidyl transferase center: Structure, function, evolution, inhibition
    • Polacek, N. & Mankin, A. S. The ribosomal peptidyl transferase center: structure, function, evolution, inhibition. Crit. Rev. Biochem. Mol. Biol 40, 285-311 (2005).
    • (2005) Crit. Rev. Biochem. Mol. Biol. , vol.40 , pp. 285-311
    • Polacek, N.1    Mankin, A.S.2
  • 5
    • 44349132844 scopus 로고    scopus 로고
    • Structural insights into the functions of the large ribosomal subunit, a major antibiotic target
    • Steitz, T. A. Structural insights into the functions of the large ribosomal subunit, a major antibiotic target. Keio J. Med 57, 1-14 (2008).
    • (2008) Keio J. Med , vol.57 , pp. 1-14
    • Steitz, T.A.1
  • 6
    • 33645465733 scopus 로고    scopus 로고
    • Antibiotics and the ribosome
    • Tenson, T. & Mankin, A. Antibiotics and the ribosome. Mol. Microbiol 59, 1664-77 (2006).
    • (2006) Mol. Microbiol , vol.59 , pp. 1664-1677
    • Tenson, T.1    Mankin, A.2
  • 7
    • 11244307407 scopus 로고    scopus 로고
    • Binding site of the bridged macrolides in the Escherichia coli ribosome
    • Xiong, L., Korkhin, Y. & Mankin, A. S. Binding site of the bridged macrolides in the Escherichia coli ribosome. Antimicrob Agents Chemother 49, 281-8 (2005).
    • (2005) Antimicrob Agents Chemother , vol.49 , pp. 281-288
    • Xiong, L.1    Korkhin, Y.2    Mankin, A.S.3
  • 8
    • 0033588103 scopus 로고    scopus 로고
    • Translational control by an upstream open reading frame in the HER-2/neu transcript
    • Child, S. J., Miller, M. K. & Geballe, A. P. Translational control by an upstream open reading frame in the HER-2/neu transcript. J. Biol. Chem 274, 24335-41 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 24335-24341
    • Child, S.J.1    Miller, M.K.2    Geballe, A.P.3
  • 9
    • 1642570293 scopus 로고    scopus 로고
    • A nascent polypeptide domain that can regulate translation elongation
    • Fang, P., Spevak, C. C., Wu, C. & Sachs, M. S. A nascent polypeptide domain that can regulate translation elongation. Proc. Natl. Acad. Sci. U. S. A 101, 4059-64 (2004).
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 4059-4064
    • Fang, P.1    Spevak, C.C.2    Wu, C.3    Sachs, M.S.4
  • 10
    • 0036893271 scopus 로고    scopus 로고
    • Inhibition of translation termination mediated by an interaction of eukaryotic release factor 1 with a nascent peptidyl-tRNA
    • Janzen, D. M., Frolova, L. & Geballe, A. P. Inhibition of translation termination mediated by an interaction of eukaryotic release factor 1 with a nascent peptidyl-tRNA. Mol. Cell. Biol 22, 8562-70 (2002).
    • (2002) Mol. Cell. Biol , vol.22 , pp. 8562-8570
    • Janzen, D.M.1    Frolova, L.2    Geballe, A.P.3
  • 11
    • 0037040411 scopus 로고    scopus 로고
    • The ribosomal exit tunnel functions as a discriminating gate
    • Nakatogawa, H. & Ito, K. The ribosomal exit tunnel functions as a discriminating gate. Cell 108, 629-36 (2002).
    • (2002) Cell , vol.108 , pp. 629-636
    • Nakatogawa, H.1    Ito, K.2
  • 12
    • 23744453365 scopus 로고    scopus 로고
    • Nascent peptide-mediated translation elongation arrest coupled with mRNA degradation in the CGS1 gene of Arabidopsis
    • Onouchi, H. et al. Nascent peptide-mediated translation elongation arrest coupled with mRNA degradation in the CGS1 gene of Arabidopsis. Genes Dev 19, 1799-810 (2005).
    • (2005) Genes Dev , vol.19 , pp. 1799-1810
    • Onouchi, H.1
  • 13
    • 0037155130 scopus 로고    scopus 로고
    • Regulated translation termination at the upstream open reading frame in s-adenosylmethionine decarboxylase mRNA
    • Raney, A., Law, G. L., Mize, G. J. & Morris, D. R. Regulated translation termination at the upstream open reading frame in s-adenosylmethionine decarboxylase mRNA. J. Biol. Chem 277, 5988-94 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 5988-5994
    • Raney, A.1    Law, G.L.2    Mize, G.J.3    Morris, D.R.4
  • 14
    • 23044445236 scopus 로고    scopus 로고
    • Features of ribosome-peptidyl-tRNA interactions essential for tryptophan induction of tna operon expression
    • Cruz-Vera, L. R., Rajagopal, S., Squires, C. & Yanofsky, C. Features of ribosome-peptidyl-tRNA interactions essential for tryptophan induction of tna operon expression. Mol. Cell 19, 333-43 (2005).
    • (2005) Mol. Cell. , vol.19 , pp. 333-343
    • Cruz-Vera, L.R.1    Rajagopal, S.2    Squires, C.3    Yanofsky, C.4
  • 15
    • 47249162502 scopus 로고    scopus 로고
    • Conserved Residues Asp16 and Pro24 of tnaC-tRNAPro Participate in Tryptophan Induction of tna Operon Expression
    • Cruz-Vera, L. R. & Yanofsky, C. Conserved Residues Asp16 and Pro24 of tnaC-tRNAPro Participate in Tryptophan Induction of tna Operon Expression. J. Bacteriol 190, 4791-97 (2008).
    • (2008) J. Bacteriol , vol.190 , pp. 4791-4797
    • Cruz-Vera, L.R.1    Yanofsky, C.2
  • 16
    • 70350443395 scopus 로고    scopus 로고
    • Tryptophan inhibits Proteus vulgaris tnaC leader peptide elongation, activating tna operon expression
    • Cruz-Vera, L. R., Yang, R. & Yanofsky, C. Tryptophan inhibits Proteus vulgaris tnaC leader peptide elongation, activating tna operon expression. J Bacteriol 191, 7001-6 (2009).
    • (2009) J Bacteriol , vol.191 , pp. 7001-7006
    • Cruz-Vera, L.R.1    Yang, R.2    Yanofsky, C.3
  • 17
    • 34247868068 scopus 로고    scopus 로고
    • Ribosomal features essential for tna operon induction: Tryptophan binding at the peptidyl transferase center
    • Cruz-Vera, L. R., New, A., Squires, C. & Yanofsky, C. Ribosomal features essential for tna operon induction: tryptophan binding at the peptidyl transferase center. J. Bacteriol 189, 3140-6 (2007).
    • (2007) J. Bacteriol , vol.189 , pp. 3140-3146
    • Cruz-Vera, L.R.1    New, A.2    Squires, C.3    Yanofsky, C.4
  • 18
    • 0034904102 scopus 로고    scopus 로고
    • Cell-free translation reconstituted with purified components
    • Shimizu, Y. et al. Cell-free translation reconstituted with purified components. Nat. Biotechnol 19, 751-5 (2001).
    • (2001) Nat. Biotechnol , vol.19 , pp. 751-755
    • Shimizu, Y.1
  • 19
    • 0030804068 scopus 로고    scopus 로고
    • Fluorescence-, isotope-or biotin-labeling of the 5 '-end of single-stranded DNA/RNA using T4 RNA ligase
    • Kinoshita, Y., Nishigaki, K. & Husimi, Y. Fluorescence-, isotope-or biotin-labeling of the 5 '-end of single-stranded DNA/RNA using T4 RNA ligase. Nucleic Acids Res 25, 3747-8 (1997).
    • (1997) Nucleic Acids Res , vol.25 , pp. 3747-3748
    • Kinoshita, Y.1    Nishigaki, K.2    Husimi, Y.3
  • 20
    • 0032227473 scopus 로고    scopus 로고
    • Y-ligation: An efficient method for ligating single-stranded DNAs and RNAs with T4 RNA ligase
    • Nishigaki, K., Taguchi, K., Kinoshita, Y., Aita, T. & Husimi, Y. Y-ligation: an efficient method for ligating single-stranded DNAs and RNAs with T4 RNA ligase. Mol Divers 4, 187-90 (1998).
    • (1998) Mol Divers , vol.4 , pp. 187-190
    • Nishigaki, K.1    Taguchi, K.2    Kinoshita, Y.3    Aita, T.4    Husimi, Y.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.