메뉴 건너뛰기




Volumn 111, Issue 46, 2014, Pages 16274-16279

Negamycin induces translational stalling and miscoding by binding to the small subunit head domain of the escherichia coli ribosome

Author keywords

Antibiotic; Fidelity; Negamycin; Ribosome; Translation

Indexed keywords

GENTAMICIN; GUANOSINE TRIPHOSPHATASE; NEGAMYCIN; RNA 16S; TETRACYCLINE; TIGECYCLINE; TRANSFER RNA; ANTIINFECTIVE AGENT; BACTERIAL RNA; DIAMINO ACID; MINOCYCLINE; TETRACYCLINE DERIVATIVE;

EID: 84911883716     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1414401111     Document Type: Article
Times cited : (36)

References (47)
  • 2
    • 42549171131 scopus 로고    scopus 로고
    • Federal funding for the study of antimicrobial resistance in nosocomial pathogens: No ESKAPE
    • Rice LB (2008) Federal funding for the study of antimicrobial resistance in nosocomial pathogens: no ESKAPE. J Infect Dis 197(8):1079-1081.
    • (2008) J Infect Dis , vol.197 , Issue.8 , pp. 1079-1081
    • Rice, L.B.1
  • 5
    • 84911917080 scopus 로고
    • Chemical studies on antibiotics and other bioactive microbial products by Prof. Hamao Umezawa
    • Maeda KO, Ohno M (1979) Chemical studies on antibiotics and other bioactive microbial products by Prof. Hamao Umezawa. Heterocycles 13(1):49-78.
    • (1979) Heterocycles , vol.13 , Issue.1 , pp. 49-78
    • Maeda, K.O.1    Ohno, M.2
  • 6
    • 10744222313 scopus 로고    scopus 로고
    • N- and C-terminal modifications of negamycin
    • Raju B, et al. (2003) N- and C-terminal modifications of negamycin. Bioorg Med Chem Lett 13(14):2413-2418.
    • (2003) Bioorg Med Chem Lett , vol.13 , Issue.14 , pp. 2413-2418
    • Raju, B.1
  • 7
    • 2442600065 scopus 로고    scopus 로고
    • Conformationally restricted analogs of deoxynegamycin
    • Raju B, et al. (2004) Conformationally restricted analogs of deoxynegamycin. Bioorg Med Chem Lett 14(12):3103-3107.
    • (2004) Bioorg Med Chem Lett , vol.14 , Issue.12 , pp. 3103-3107
    • Raju, B.1
  • 8
    • 0014916977 scopus 로고
    • Mechanism of action of negamycin in Escherichia coli K12. I. Inhibition of initiation of protein synthesis
    • Mizuno S, Nitta K, Umezawa H (1970) Mechanism of action of negamycin in Escherichia coli K12. I. Inhibition of initiation of protein synthesis. J Antibiot (Tokyo) 23(12):581-588.
    • (1970) J Antibiot (Tokyo) , vol.23 , Issue.12 , pp. 581-588
    • Mizuno, S.1    Nitta, K.2    Umezawa, H.3
  • 10
    • 0014917012 scopus 로고
    • Mechanism of action of negamycin in Escherichia coli K12. II. Miscoding activity in polypeptide synthesis directed by snythetic polynucleotide
    • Mizuno S, Nitta K, Umezawa H (1970) Mechanism of action of negamycin in Escherichia coli K12. II. Miscoding activity in polypeptide synthesis directed by snythetic polynucleotide. J Antibiot (Tokyo) 23(12):589-594.
    • (1970) J Antibiot (Tokyo) , vol.23 , Issue.12 , pp. 589-594
    • Mizuno, S.1    Nitta, K.2    Umezawa, H.3
  • 11
    • 0016299512 scopus 로고
    • Negamycin inhibits termination of protein synthesis directed by phage f2 RNA in vitro
    • Uehara Y, Hori M, Umezawa H (1974) Negamycin inhibits termination of protein synthesis directed by phage f2 RNA in vitro. Biochim Biophys Acta 374(1):82-95.
    • (1974) Biochim Biophys Acta , vol.374 , Issue.1 , pp. 82-95
    • Uehara, Y.1    Hori, M.2    Umezawa, H.3
  • 12
    • 0017092883 scopus 로고
    • Inhibitory effect of negamycin on polysomal ribosomes of Escherichia coli
    • Uehara Y, Hori M, Umezawa H (1976) Inhibitory effect of negamycin on polysomal ribosomes of Escherichia coli. Biochim Biophys Acta 447(4):406-412.
    • (1976) Biochim Biophys Acta , vol.447 , Issue.4 , pp. 406-412
    • Uehara, Y.1    Hori, M.2    Umezawa, H.3
  • 13
    • 0017080387 scopus 로고
    • Specific inhibition of the termination process of protein synthesis by negamycin
    • Uehara Y, Hori M, Umezawa H (1976) Specific inhibition of the termination process of protein synthesis by negamycin. Biochim Biophys Acta 442(2):251-262.
    • (1976) Biochim Biophys Acta , vol.442 , Issue.2 , pp. 251-262
    • Uehara, Y.1    Hori, M.2    Umezawa, H.3
  • 14
    • 36749023383 scopus 로고    scopus 로고
    • Negamycin binds to the wall of the nascent chain exit tunnel of the 50S ribosomal subunit
    • Schroeder SJ, Blaha G, Moore PB (2007) Negamycin binds to the wall of the nascent chain exit tunnel of the 50S ribosomal subunit. Antimicrob Agents Chemother 51(12):4462-4465.
    • (2007) Antimicrob Agents Chemother , vol.51 , Issue.12 , pp. 4462-4465
    • Schroeder, S.J.1    Blaha, G.2    Moore, P.B.3
  • 15
    • 77954764349 scopus 로고    scopus 로고
    • Antibiotic selectivity for prokaryotic vs. Eukaryotic decoding sites
    • Xie Y, Dix AV, Tor Y (2010) Antibiotic selectivity for prokaryotic vs. eukaryotic decoding sites. Chem Commun (Camb) 46(30):5542-5544.
    • (2010) Chem Commun (Camb) , vol.46 , Issue.30 , pp. 5542-5544
    • Xie, Y.1    Dix, A.V.2    Tor, Y.3
  • 16
    • 0347993773 scopus 로고    scopus 로고
    • Negamycin restores dystrophin expression in skeletal and cardiac muscles of mdx mice
    • Arakawa M, et al. (2003) Negamycin restores dystrophin expression in skeletal and cardiac muscles of mdx mice. J Biochem 134(5):751-758.
    • (2003) J Biochem , vol.134 , Issue.5 , pp. 751-758
    • Arakawa, M.1
  • 17
    • 0035900647 scopus 로고    scopus 로고
    • When the message goes awry: Disease-producing mutations that influence mRNA content and performance
    • Mendell JT, Dietz HC (2001) When the message goes awry: Disease-producing mutations that influence mRNA content and performance. Cell 107(4):411-414.
    • (2001) Cell , vol.107 , Issue.4 , pp. 411-414
    • Mendell, J.T.1    Dietz, H.C.2
  • 18
    • 84867328079 scopus 로고    scopus 로고
    • Pharmaceutical therapies to recode nonsense mutations in inherited diseases
    • Lee HL, Dougherty JP (2012) Pharmaceutical therapies to recode nonsense mutations in inherited diseases. Pharmacol Ther 136(2):227-266.
    • (2012) Pharmacol Ther , vol.136 , Issue.2 , pp. 227-266
    • Lee, H.L.1    Dougherty, J.P.2
  • 20
    • 77954814800 scopus 로고    scopus 로고
    • Conformational sampling of aminoacyl-tRNA during selection on the bacterial ribosome
    • Geggier P, et al. (2010) Conformational sampling of aminoacyl-tRNA during selection on the bacterial ribosome. J Mol Biol 399(4):576-595.
    • (2010) J Mol Biol , vol.399 , Issue.4 , pp. 576-595
    • Geggier, P.1
  • 21
    • 84874605802 scopus 로고    scopus 로고
    • Structural basis for potent inhibitory activity of the antibiotic tigecycline during protein synthesis
    • Jenner L, et al. (2013) Structural basis for potent inhibitory activity of the antibiotic tigecycline during protein synthesis. Proc Natl Acad Sci USA 110(10):3812-3816.
    • (2013) Proc Natl Acad Sci USA , vol.110 , Issue.10 , pp. 3812-3816
    • Jenner, L.1
  • 22
    • 70549091101 scopus 로고    scopus 로고
    • Total synthesis of (+)-negamycin and its 5-epi-derivative
    • Nishiguchi S, et al. (2010) Total synthesis of (+)-negamycin and its 5-epi-derivative. Tetrahedron 66(1):314-320.
    • (2010) Tetrahedron , vol.66 , Issue.1 , pp. 314-320
    • Nishiguchi, S.1
  • 23
    • 84887462372 scopus 로고    scopus 로고
    • Tools for characterizing bacterial protein synthesis inhibitors
    • Orelle C, et al. (2013) Tools for characterizing bacterial protein synthesis inhibitors. Antimicrob Agents Chemother 57(12):5994-6004.
    • (2013) Antimicrob Agents Chemother , vol.57 , Issue.12 , pp. 5994-6004
    • Orelle, C.1
  • 24
    • 0023238983 scopus 로고
    • Interaction of antibiotics with functional sites in 16S ribosomal RNA
    • Moazed D, Noller HF (1987) Interaction of antibiotics with functional sites in 16S ribosomal RNA. Nature 327(6121):389-394.
    • (1987) Nature , vol.327 , Issue.6121 , pp. 389-394
    • Moazed, D.1    Noller, H.F.2
  • 25
    • 0036035221 scopus 로고    scopus 로고
    • The tetracycline resistance protein Tet (o) perturbs the conformation of the ribosomal decoding centre
    • Connell SR, et al. (2002) The tetracycline resistance protein Tet (o) perturbs the conformation of the ribosomal decoding centre. Mol Microbiol 45(6):1463-1472.
    • (2002) Mol Microbiol , vol.45 , Issue.6 , pp. 1463-1472
    • Connell, S.R.1
  • 26
    • 0034704217 scopus 로고    scopus 로고
    • The structural basis for the action of the antibiotics tetracycline, pactamycin, and hygromycin B on the 30S ribosomal subunit
    • Brodersen DE, et al. (2000) The structural basis for the action of the antibiotics tetracycline, pactamycin, and hygromycin B on the 30S ribosomal subunit. Cell 103(7):1143-1154.
    • (2000) Cell , vol.103 , Issue.7 , pp. 1143-1154
    • Brodersen, D.E.1
  • 27
    • 69249112231 scopus 로고    scopus 로고
    • Structures of the ribosome in intermediate states of ratcheting
    • Zhang W, Dunkle JA, Cate JH (2009) Structures of the ribosome in intermediate states of ratcheting. Science 325(5943):1014-1017.
    • (2009) Science , vol.325 , Issue.5943 , pp. 1014-1017
    • Zhang, W.1    Dunkle, J.A.2    Cate, J.H.3
  • 28
    • 84860123958 scopus 로고    scopus 로고
    • Target- and resistance-based mechanistic studies with TP-434, a novel fluorocycline antibiotic
    • Grossman TH, et al. (2012) Target- and resistance-based mechanistic studies with TP-434, a novel fluorocycline antibiotic. Antimicrob Agents Chemother 56(5):2559-2564.
    • (2012) Antimicrob Agents Chemother , vol.56 , Issue.5 , pp. 2559-2564
    • Grossman, T.H.1
  • 29
    • 84867656705 scopus 로고    scopus 로고
    • Structural basis for TetM-mediated tetracycline resistance
    • Dönhöfer A, et al. (2012) Structural basis for TetM-mediated tetracycline resistance. Proc Natl Acad Sci USA 109(42):16900-16905.
    • (2012) Proc Natl Acad Sci USA , vol.109 , Issue.42 , pp. 16900-16905
    • Dönhöfer, A.1
  • 30
    • 0022544304 scopus 로고
    • Streptococcal tetracycline resistance mediated at the level of protein synthesis
    • Burdett V (1986) Streptococcal tetracycline resistance mediated at the level of protein synthesis. J Bacteriol 165(2):564-569.
    • (1986) J Bacteriol , vol.165 , Issue.2 , pp. 564-569
    • Burdett, V.1
  • 31
    • 84866055435 scopus 로고    scopus 로고
    • Allosteric control of the ribosome by small-molecule antibiotics
    • Wang L, et al. (2012) Allosteric control of the ribosome by small-molecule antibiotics. Nat Struct Mol Biol 19(9):957-963.
    • (2012) Nat Struct Mol Biol , vol.19 , Issue.9 , pp. 957-963
    • Wang, L.1
  • 32
    • 78649830457 scopus 로고    scopus 로고
    • Correlated conformational events in EF-G and the ribosome regulate translocation
    • Munro JB, Wasserman MR, Altman RB, Wang L, Blanchard SC (2010) Correlated conformational events in EF-G and the ribosome regulate translocation. Nat Struct Mol Biol 17(12):1470-1477.
    • (2010) Nat Struct Mol Biol , vol.17 , Issue.12 , pp. 1470-1477
    • Munro, J.B.1    Wasserman, M.R.2    Altman, R.B.3    Wang, L.4    Blanchard, S.C.5
  • 33
    • 84876053851 scopus 로고    scopus 로고
    • Mechanistic insights into antibiotic action on the ribosome through single-molecule fluorescence imaging
    • Wang L, Wasserman MR, Feldman MB, Altman RB, Blanchard SC (2011) Mechanistic insights into antibiotic action on the ribosome through single-molecule fluorescence imaging. Ann N Y Acad Sci 1241:E1-E16.
    • (2011) Ann N Y Acad Sci , vol.1241 , pp. E1-E16
    • Wang, L.1    Wasserman, M.R.2    Feldman, M.B.3    Altman, R.B.4    Blanchard, S.C.5
  • 34
    • 77950391683 scopus 로고    scopus 로고
    • Aminoglycoside activity observed on single pre-translocation ribosome complexes
    • Feldman MB, Terry DS, Altman RB, Blanchard SC (2010) Aminoglycoside activity observed on single pre-translocation ribosome complexes. Nat Chem Biol 6(1):54-62.
    • (2010) Nat Chem Biol , vol.6 , Issue.1 , pp. 54-62
    • Feldman, M.B.1    Terry, D.S.2    Altman, R.B.3    Blanchard, S.C.4
  • 35
    • 84861381646 scopus 로고    scopus 로고
    • How should we think about the ribosome?
    • Moore PB (2012) How should we think about the ribosome? Annu Rev Biophys 41:1-19.
    • (2012) Annu Rev Biophys , vol.41 , pp. 1-19
    • Moore, P.B.1
  • 38
    • 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 JA, Xiong L, Mankin AS, Cate JH (2010) Structures of the Escherichia coli ribosome with antibiotics bound near the peptidyl transferase center explain spectra of drug action. Proc Natl Acad Sci USA 107(40):17152-17157.
    • (2010) Proc Natl Acad Sci USA , vol.107 , Issue.40 , pp. 17152-17157
    • Dunkle, J.A.1    Xiong, L.2    Mankin, A.S.3    Cate, J.H.4
  • 39
    • 17744377418 scopus 로고    scopus 로고
    • Crystal structures of complexes of the small ribosomal subunit with tetracycline, edeine and IF3
    • Pioletti M, et al. (2001) Crystal structures of complexes of the small ribosomal subunit with tetracycline, edeine and IF3. EMBO J 20(8):1829-1839.
    • (2001) EMBO J , vol.20 , Issue.8 , pp. 1829-1839
    • Pioletti, M.1
  • 40
    • 32844459761 scopus 로고    scopus 로고
    • Interactions of designer antibiotics and the bacterial ribosomal aminoacyl-tRNA site
    • Murray JB, et al. (2006) Interactions of designer antibiotics and the bacterial ribosomal aminoacyl-tRNA site. Chem Biol 13(2):129-138.
    • (2006) Chem Biol , vol.13 , Issue.2 , pp. 129-138
    • Murray, J.B.1
  • 41
    • 0034086680 scopus 로고    scopus 로고
    • Preparation of functional ribosomal complexes and effect of buffer conditions on tRNA positions observed by cryoelectron microscopy
    • Blaha G, et al. (2000) Preparation of functional ribosomal complexes and effect of buffer conditions on tRNA positions observed by cryoelectron microscopy. Methods Enzymol 317:292-309.
    • (2000) Methods Enzymol , vol.317 , pp. 292-309
    • Blaha, G.1
  • 44
    • 79953733151 scopus 로고    scopus 로고
    • Data processing and analysis with the autoPROC toolbox
    • Vonrhein C, et al. (2011) Data processing and analysis with the autoPROC toolbox. Acta Crystallogr D Biol Crystallogr 67(Pt 4):293-302.
    • (2011) Acta Crystallogr D Biol Crystallogr , vol.67 , pp. 293-302
    • Vonrhein, C.1
  • 46
    • 77957946297 scopus 로고    scopus 로고
    • Global Phasing Ltd., Cambridge, UK
    • Bricogne G, et al. (2011) Buster V2.11.5 (Global Phasing Ltd., Cambridge, UK).
    • (2011) Buster V2.11.5
    • Bricogne, G.1
  • 47
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams PD, et al. (2010) PHENIX: A comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr D Biol Crystallogr 66(Pt 2):213-221.
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , pp. 213-221
    • Adams, P.D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.