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Volumn 286, Issue 2, 1999, Pages 375-387

Sites of interaction of streptogramin A and B antibiotics in the peptidyl transferase loop of 23 S rRNA and the synergism of their inhibitory mechanisms

Author keywords

Bacillus megaterium; Halobacterium halobium; Peptidyl transferase loop; rRNA footprinting; Streptogramin A and B

Indexed keywords

DALFOPRISTIN; MIKAMYCIN B; PEPTIDYLTRANSFERASE; PRISTINAMYCIN; RNA 23S;

EID: 0033582599     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.2509     Document Type: Article
Times cited : (70)

References (40)
  • 1
    • 0029134517 scopus 로고
    • Diversity among the Gram-positive acetyltransferases inactivating streptogramin A and structurally related compounds and characterization of a new staphylococcal determinant, vatB
    • Allignet J., el Solh N. Diversity among the Gram-positive acetyltransferases inactivating streptogramin A and structurally related compounds and characterization of a new staphylococcal determinant, vatB. Antimicrob. Agents Chemother. 39:1995;2027-2036.
    • (1995) Antimicrob. Agents Chemother. , vol.39 , pp. 2027-2036
    • Allignet, J.1    El Solh, N.2
  • 2
    • 0030782614 scopus 로고    scopus 로고
    • Characterization of a new staphylococcal gene, vgaB, encoding a putative ABC transporter conferring resistance to streptogramin A and related compounds
    • Allignet J., el Solh N. Characterization of a new staphylococcal gene, vgaB, encoding a putative ABC transporter conferring resistance to streptogramin A and related compounds. Gene. 202:1997;133-138.
    • (1997) Gene , vol.202 , pp. 133-138
    • Allignet, J.1    El Solh, N.2
  • 3
    • 0002124045 scopus 로고
    • Peptidyl transfease inhibitors: Structure-activity relationship analysis by chemical modification
    • W. Hill, A. Dahlberg, R. A. Garrett, P. Moore, D. Schlessinger, & J. Warner. Washington: American Society of Microbiology
    • Ballesta J. P. G., Lázaro E. Peptidyl transfease inhibitors: structure-activity relationship analysis by chemical modification. Hill W., Dahlberg A., Garrett R. A., Moore P., Schlessinger D., Warner J. The Ribosome: Structure, Function and Evolution. 1990;502-510 American Society of Microbiology, Washington.
    • (1990) The Ribosome: Structure, Function and Evolution , pp. 502-510
    • Ballesta, J.P.G.1    Lázaro, E.2
  • 4
    • 0040843291 scopus 로고
    • Mitochondrial DNA of chloramphenicol-resistant mouse cells contains a single nucleotide change in the region encoding the 3′-end of the large rRNA
    • Blanc H., Wright C. T., Bibb M. J., Wallace D. C., Clayton D. A. Mitochondrial DNA of chloramphenicol-resistant mouse cells contains a single nucleotide change in the region encoding the 3′-end of the large rRNA. Proc. Natl Acad. Sci. USA. 78:1981;3789-3793.
    • (1981) Proc. Natl Acad. Sci. USA , vol.78 , pp. 3789-3793
    • Blanc, H.1    Wright, C.T.2    Bibb, M.J.3    Wallace, D.C.4    Clayton, D.A.5
  • 5
    • 0021167328 scopus 로고
    • The action of virginiamycin M on the acceptor, donor and catalytic sites of peptidyl transferase
    • Chinali G., Moureau P., Cocito C. The action of virginiamycin M on the acceptor, donor and catalytic sites of peptidyl transferase. J. Biol. Chem. 259:1984;9563-9568.
    • (1984) J. Biol. Chem. , vol.259 , pp. 9563-9568
    • Chinali, G.1    Moureau, P.2    Cocito, C.3
  • 7
    • 0017334687 scopus 로고
    • Synergistic interaction of the streptogramins with the ribosome
    • Contreras A., Vázquez D. Synergistic interaction of the streptogramins with the ribosome. Eur. J. Biochem. 74:1977;549-551.
    • (1977) Eur. J. Biochem. , vol.74 , pp. 549-551
    • Contreras, A.1    Vázquez, D.2
  • 8
    • 0024103141 scopus 로고
    • Point mutations in the 23 S rRNA genes of four lincomycin resistant Nicotiana plumbaginifola mutants could provide new selectable markers for chloroplast transformation
    • Cseplö A., Etzold T., Schell J., Schreier P. H. Point mutations in the 23 S rRNA genes of four lincomycin resistant Nicotiana plumbaginifola mutants could provide new selectable markers for chloroplast transformation. Mol. Gen. Genet. 214:1988;295-299.
    • (1988) Mol. Gen. Genet. , vol.214 , pp. 295-299
    • Cseplö, A.1    Etzold, T.2    Schell, J.3    Schreier, P.H.4
  • 9
    • 0002331708 scopus 로고
    • Recognition sites for antibiotics within rRNA
    • W. Hill, A. Dahlberg, R. A. Garrett, P. Moore, D. Schlessinger, & J. Warner. Washington: American Society of Microbiology
    • Cundliffe E. Recognition sites for antibiotics within rRNA. Hill W., Dahlberg A., Garrett R. A., Moore P., Schlessinger D., Warner J. The Ribosome: Structure, Function and Evolution. 1990;479-490 American Society of Microbiology, Washington.
    • (1990) The Ribosome: Structure, Function and Evolution , pp. 479-490
    • Cundliffe, E.1
  • 10
    • 0017897566 scopus 로고
    • Characterisation of the binding of virginiamycin S to Escherichia coli ribosomes
    • de Bethune M. P., Nierhaus K. H. Characterisation of the binding of virginiamycin S to Escherichia coli ribosomes. Eur. J. Biochem. 86:1978;187-191.
    • (1978) Eur. J. Biochem. , vol.86 , pp. 187-191
    • De Bethune, M.P.1    Nierhaus, K.H.2
  • 11
    • 0024453356 scopus 로고
    • The molecular basis of the inhibitory activities of type A and type B synergimycins and related antibiotics on ribosomes
    • Di Giambattista M., Chinali G., Cocito C. The molecular basis of the inhibitory activities of type A and type B synergimycins and related antibiotics on ribosomes. J. Antimicrob. Chemother. 24:1989;485-507.
    • (1989) J. Antimicrob. Chemother. , vol.24 , pp. 485-507
    • Di Giambattista, M.1    Chinali, G.2    Cocito, C.3
  • 12
    • 0025090786 scopus 로고
    • Affinity labeling of the virginiamycin S binding site on bacterial ribosome
    • Di Giambattista M., Nyssen E., Pecher A., Cocito C. Affinity labeling of the virginiamycin S binding site on bacterial ribosome. Biochemistry. 29:1990;9203-9211.
    • (1990) Biochemistry , vol.29 , pp. 9203-9211
    • Di Giambattista, M.1    Nyssen, E.2    Pecher, A.3    Cocito, C.4
  • 13
    • 0018903049 scopus 로고
    • Sequence of the intron and flanking exons of the mitochondrial 21 S rRNA gene of yeast strains having different alleles at the omega and rib-1 loci
    • Dujon B. Sequence of the intron and flanking exons of the mitochondrial 21 S rRNA gene of yeast strains having different alleles at the omega and rib-1 loci. Cell. 20:1980;185-197.
    • (1980) Cell , vol.20 , pp. 185-197
    • Dujon, B.1
  • 16
    • 0031566952 scopus 로고    scopus 로고
    • Mutations at nucleotides G2251 and U2585 of 23 S rRNA perturb the peptidyl transferase center of the ribosome
    • Green R., Samaha R. R., Noller H. F. Mutations at nucleotides G2251 and U2585 of 23 S rRNA perturb the peptidyl transferase center of the ribosome. J. Mol. Biol. 266:1997;40-50.
    • (1997) J. Mol. Biol. , vol.266 , pp. 40-50
    • Green, R.1    Samaha, R.R.2    Noller, H.F.3
  • 17
    • 0023139432 scopus 로고
    • 23S rRNA mutations in halobacteria conferring resistance to the anti-80S ribosome trargeted antibiotic anisomycin
    • Hummel H., Böck A. 23S rRNA mutations in halobacteria conferring resistance to the anti-80S ribosome trargeted antibiotic anisomycin. Nucl. Acids Res. 15:1987;2431-2443.
    • (1987) Nucl. Acids Res. , vol.15 , pp. 2431-2443
    • Hummel, H.1    Böck, A.2
  • 18
    • 0030904329 scopus 로고    scopus 로고
    • Movement of the 3′-end of tRNA through the peptidyl transferase centre and its inhibition by antibiotics
    • Kirillov S., Porse B. T., Vester B., Woolley P., Garrett R. A. Movement of the 3′-end of tRNA through the peptidyl transferase centre and its inhibition by antibiotics. FEBS Letters. 406:1997;223-233.
    • (1997) FEBS Letters , vol.406 , pp. 223-233
    • Kirillov, S.1    Porse, B.T.2    Vester, B.3    Woolley, P.4    Garrett, R.A.5
  • 19
    • 0030590237 scopus 로고    scopus 로고
    • A sparsomycin-resistant mutant of Halobacterium salinarium lacks a modification at nucleotide U2603 in the peptidyl transferase center of 23 S rRNA
    • Lázaro E., Rodriguez-Fonseca C., Porse B., Ure ñ D., Garrett R. A., Ballesta J. P. G. A sparsomycin-resistant mutant of Halobacterium salinarium lacks a modification at nucleotide U2603 in the peptidyl transferase center of 23 S rRNA. J. Mol. Biol. 261:1996;231-238.
    • (1996) J. Mol. Biol. , vol.261 , pp. 231-238
    • Lázaro, E.1    Rodriguez-Fonseca, C.2    Porse, B.3    Ure Ñ., D.4    Garrett, R.A.5    Ballesta, J.P.G.6
  • 20
    • 0028269333 scopus 로고
    • A conserved secondary structural motif in 23 S rRNA defines the site of interaction of amicetin, a universal inhibitor of peptide bond formation
    • Leviev I. G., Rodriguez-Fonseca C., Phan H., Garrett R. A., Heilek G., Noller H. F., Mankin A. S. A conserved secondary structural motif in 23 S rRNA defines the site of interaction of amicetin, a universal inhibitor of peptide bond formation. EMBO J. 13:1994;1682-1686.
    • (1994) EMBO J. , vol.13 , pp. 1682-1686
    • Leviev, I.G.1    Rodriguez-Fonseca, C.2    Phan, H.3    Garrett, R.A.4    Heilek, G.5    Noller, H.F.6    Mankin, A.S.7
  • 21
    • 0025892855 scopus 로고
    • Chloramphenicol resistance mutations in the single 23 S rRNA gene of the archaeon Halobacterium halobium
    • Mankin A. S., Garrett R. A. Chloramphenicol resistance mutations in the single 23 S rRNA gene of the archaeon Halobacterium halobium. J. Bacteriol. 173:1991;3559-3563.
    • (1991) J. Bacteriol. , vol.173 , pp. 3559-3563
    • Mankin, A.S.1    Garrett, R.A.2
  • 22
    • 0028134851 scopus 로고
    • Cross-hypersensitivity effects of mutations in 23 S rRNA yield insight into aminoacyl-tRNA binding
    • Mankin A. S., Leviev I., Garrett R. A. Cross-hypersensitivity effects of mutations in 23 S rRNA yield insight into aminoacyl-tRNA binding. J. Mol. Biol. 244:1994;151-157.
    • (1994) J. Mol. Biol. , vol.244 , pp. 151-157
    • Mankin, A.S.1    Leviev, I.2    Garrett, R.A.3
  • 23
    • 0023604799 scopus 로고
    • Chloramphenicol, erythromycin, carbomycin and vernamycin B protect overlapping sites in the peptidyl transferase region of 23 S rRNA
    • Moazed D., Noller H. F. Chloramphenicol, erythromycin, carbomycin and vernamycin B protect overlapping sites in the peptidyl transferase region of 23 S rRNA. Biochimie. 69:1987;879-884.
    • (1987) Biochimie , vol.69 , pp. 879-884
    • Moazed, D.1    Noller, H.F.2
  • 24
    • 0024334898 scopus 로고
    • Interaction of tRNA with 23 S rRNA in the ribosomal A, P, and E sites
    • Moazed D., Noller H. F. Interaction of tRNA with 23 S rRNA in the ribosomal A, P, and E sites. Cell. 57:1989;585-597.
    • (1989) Cell , vol.57 , pp. 585-597
    • Moazed, D.1    Noller, H.F.2
  • 25
    • 0014219788 scopus 로고
    • Ribosome-catalyzed peptidyl transfer: Effects of some inhibitors of protein synthesis
    • Monro R. E., Vázquez D. Ribosome-catalyzed peptidyl transfer: effects of some inhibitors of protein synthesis. J. Mol. Biol. 28:1967;161-165.
    • (1967) J. Mol. Biol. , vol.28 , pp. 161-165
    • Monro, R.E.1    Vázquez, D.2
  • 26
    • 0019143485 scopus 로고
    • Lasting damage to bacterial ribosomes by reversibly bound virginiamycin M
    • Parfait R., Cocito C. Lasting damage to bacterial ribosomes by reversibly bound virginiamycin M. Proc. Natl Acad. Sci. USA. 77:1980;5492-5496.
    • (1980) Proc. Natl Acad. Sci. USA , vol.77 , pp. 5492-5496
    • Parfait, R.1    Cocito, C.2
  • 27
    • 0029011424 scopus 로고
    • Mapping important nucleotides in the peptidyl transferase centre of 23 S rRNA using a random mutagenesis approach
    • Porse B. T., Garrett R. A. Mapping important nucleotides in the peptidyl transferase centre of 23 S rRNA using a random mutagenesis approach. J. Mol. Biol. 249:1995;1-10.
    • (1995) J. Mol. Biol. , vol.249 , pp. 1-10
    • Porse, B.T.1    Garrett, R.A.2
  • 29
    • 0032899549 scopus 로고    scopus 로고
    • UV-induced modifications in the peptidyl transferase loop of 23 S rRNA dependent on binding of the streptogramin B antibiotic, pristinamycin IA
    • Porse B. T., Kirillov S. V., Awayez M., Garrett R. A. UV-induced modifications in the peptidyl transferase loop of 23 S rRNA dependent on binding of the streptogramin B antibiotic, pristinamycin IA. RNA. 1999a.
    • (1999) RNA
    • Porse, B.T.1    Kirillov, S.V.2    Awayez, M.3    Garrett, R.A.4
  • 30
    • 0033583095 scopus 로고    scopus 로고
    • The antibiotic micrococcin acts on protein L11 in the ribosomal GTPase centre
    • Porse B. T., Cundliffe E., Garrett R. A. The antibiotic micrococcin acts on protein L11 in the ribosomal GTPase centre. J. Mol. Biol. 1999b.
    • (1999) J. Mol. Biol.
    • Porse, B.T.1    Cundliffe, E.2    Garrett, R.A.3
  • 31
    • 0028924641 scopus 로고
    • Fine structure of the peptidyl transferase centre on 23 S-like rRNAs deduced from chemical probing of antibiotic-ribosome complexes
    • Rodriguez-Fonseca C., Amils R., Garrett R. A. Fine structure of the peptidyl transferase centre on 23 S-like rRNAs deduced from chemical probing of antibiotic-ribosome complexes. J. Mol. Biol. 247:1995;224-235.
    • (1995) J. Mol. Biol. , vol.247 , pp. 224-235
    • Rodriguez-Fonseca, C.1    Amils, R.2    Garrett, R.A.3
  • 32
    • 12644274577 scopus 로고    scopus 로고
    • Mutational analysis of two highly conserved UGG sequences of 23 S rRNA from Escherichia coli
    • Spahn C. M. T., Remme J., Schafer M. A., Nierhaus K. H. Mutational analysis of two highly conserved UGG sequences of 23 S rRNA from Escherichia coli. J. Biol. Chem. 271:1996;32849-32856.
    • (1996) J. Biol. Chem. , vol.271 , pp. 32849-32856
    • Spahn, C.M.T.1    Remme, J.2    Schafer, M.A.3    Nierhaus, K.H.4
  • 33
    • 0029055199 scopus 로고
    • Mapping the path of the nascent peptide chain through the 23 S RNA in the 50 S ribosomal subunit
    • Stade K., Junke N., Brimacombe R. Mapping the path of the nascent peptide chain through the 23 S RNA in the 50 S ribosomal subunit. Nucl. Acids Res. 23:1995;2371-2380.
    • (1995) Nucl. Acids Res. , vol.23 , pp. 2371-2380
    • Stade, K.1    Junke, N.2    Brimacombe, R.3
  • 34
    • 0030590258 scopus 로고    scopus 로고
    • Mutations in the peptidyl transferase center of 23 S rRNA reveal the site of action of sparsomycin, a universal inhibitor of translation
    • Tan G. T., DeBlasio A., Mankin A. S. Mutations in the peptidyl transferase center of 23 S rRNA reveal the site of action of sparsomycin, a universal inhibitor of translation. J. Mol. Biol. 261:1996;222-230.
    • (1996) J. Mol. Biol. , vol.261 , pp. 222-230
    • Tan, G.T.1    DeBlasio, A.2    Mankin, A.S.3
  • 35
    • 0026671180 scopus 로고
    • The role of rRNA bases in the interaction of peptidyl transferase inhibitors with bacterial ribosomes
    • Vanuffel P., Di Giambattista M., Cocito C. The role of rRNA bases in the interaction of peptidyl transferase inhibitors with bacterial ribosomes. J. Biol. Chem. 267:1992;16114-16120.
    • (1992) J. Biol. Chem. , vol.267 , pp. 16114-16120
    • Vanuffel, P.1    Di Giambattista, M.2    Cocito, C.3
  • 36
    • 0028099297 scopus 로고
    • Chemical probing of a virginiamycin M-promoted conformational change of the peptidyl transferase domain
    • Vanuffel P., Di Giambattista M., Cocito C. Chemical probing of a virginiamycin M-promoted conformational change of the peptidyl transferase domain. Nucl. Acids Res. 22:1994;4449-4453.
    • (1994) Nucl. Acids Res. , vol.22 , pp. 4449-4453
    • Vanuffel, P.1    Di Giambattista, M.2    Cocito, C.3
  • 39
    • 0024114860 scopus 로고
    • The importance of highly conserved nucleotides in the binding region of chloramphenicol at the peptidyl transfer center of Escherichia coli 23 S rRNA
    • Vester B., Garrett R. A. The importance of highly conserved nucleotides in the binding region of chloramphenicol at the peptidyl transfer center of Escherichia coli 23 S rRNA. EMBO J. 7:1988;3577-3587.
    • (1988) EMBO J. , vol.7 , pp. 3577-3587
    • Vester, B.1    Garrett, R.A.2


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