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Volumn 91, Issue 8, 2009, Pages 989-995

Cis-acting resistance peptides reveal dual ribosome inhibitory action of the macrolide josamycin

Author keywords

Inhibition; Josamycin; Macrolide; Protein synthesis; Resistance

Indexed keywords

DIPEPTIDE; ERYTHROMYCIN; JOSAMYCIN; MACROLIDE; MESSENGER RNA; PEPTIDE DERIVATIVE; RIBONUCLEASE; TRANSFER RNA;

EID: 67649450458     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2009.05.002     Document Type: Article
Times cited : (10)

References (40)
  • 2
    • 0035950132 scopus 로고    scopus 로고
    • Structural basis for the interaction of antibiotics with the peptidyl transferase centre in eubacteria
    • Schlunzen F., Zarivach R., Harms J., Bashan A., Tocilj A., Albrecht R., et al. Structural basis for the interaction of antibiotics with the peptidyl transferase centre in eubacteria. Nature 413 (2001) 814-821
    • (2001) Nature , vol.413 , pp. 814-821
    • Schlunzen, F.1    Zarivach, R.2    Harms, J.3    Bashan, A.4    Tocilj, A.5    Albrecht, R.6
  • 3
    • 0036342198 scopus 로고    scopus 로고
    • The structures of four macrolide antibiotics bound to the large ribosomal subunit
    • Hansen J.L., Ippolito J.A., Ban N., Nissen P., Moore P.B., and Steitz T.A. The structures of four macrolide antibiotics bound to the large ribosomal subunit. Mol. Cell 10 (2002) 117-128
    • (2002) Mol. Cell , vol.10 , pp. 117-128
    • Hansen, J.L.1    Ippolito, J.A.2    Ban, N.3    Nissen, P.4    Moore, P.B.5    Steitz, T.A.6
  • 4
    • 17444421169 scopus 로고    scopus 로고
    • Structures of MLS(B)K antibiotics bound to mutated large ribosomal subunits provide a structural explanation for resistance
    • Tu D., Blaha G., Moore P.B., and Steitz T.A. Structures of MLS(B)K antibiotics bound to mutated large ribosomal subunits provide a structural explanation for resistance. Cell 121 (2005) 257-270
    • (2005) Cell , vol.121 , pp. 257-270
    • Tu, D.1    Blaha, G.2    Moore, P.B.3    Steitz, T.A.4
  • 5
    • 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., and Ehrenberg M. The mechanism of action of macrolides, lincosamides and streptogramin B reveals the nascent peptide exit path in the ribosome. J. Mol. Biol. 330 (2003) 1005-1014
    • (2003) J. Mol. Biol. , vol.330 , pp. 1005-1014
    • Tenson, T.1    Lovmar, M.2    Ehrenberg, M.3
  • 6
    • 11144238888 scopus 로고    scopus 로고
    • Kinetics of macrolide action: the josamycin and erythromycin cases
    • Lovmar M., Tenson T., and Ehrenberg M. Kinetics of macrolide action: the josamycin and erythromycin cases. J. Biol. Chem. 279 (2004) 53506-53515
    • (2004) J. Biol. Chem. , vol.279 , pp. 53506-53515
    • Lovmar, M.1    Tenson, T.2    Ehrenberg, M.3
  • 7
    • 0034406527 scopus 로고    scopus 로고
    • Inhibition of the ribosomal peptidyl transferase reaction by the mycarose moiety of the antibiotics carbomycin, spiramycin and tylosin
    • Poulsen S.M., Kofoed C., and Vester B. Inhibition of the ribosomal peptidyl transferase reaction by the mycarose moiety of the antibiotics carbomycin, spiramycin and tylosin. J. Mol. Biol. 304 (2000) 471-481
    • (2000) J. Mol. Biol. , vol.304 , pp. 471-481
    • Poulsen, S.M.1    Kofoed, C.2    Vester, B.3
  • 8
    • 0020322533 scopus 로고
    • Erythromycin, carbomycin, and spiramycin inhibit protein synthesis by stimulating the dissociation of peptidyl-tRNA from ribosomes
    • Menninger J.R., and Otto D.P. Erythromycin, carbomycin, and spiramycin inhibit protein synthesis by stimulating the dissociation of peptidyl-tRNA from ribosomes. Antimicrobial. Agents Chemother. 21 (1982) 811-818
    • (1982) Antimicrobial. Agents Chemother. , vol.21 , pp. 811-818
    • Menninger, J.R.1    Otto, D.P.2
  • 9
    • 0016710554 scopus 로고
    • Release of (oligo) peptidyl-tRNA from ribosomes by erythromycin A
    • Otaka T., and Kaji A. Release of (oligo) peptidyl-tRNA from ribosomes by erythromycin A. Proc. Natl. Acad. Sci. U.S.A. 72 (1975) 2649-2652
    • (1975) Proc. Natl. Acad. Sci. U.S.A. , vol.72 , pp. 2649-2652
    • Otaka, T.1    Kaji, A.2
  • 10
    • 0038811884 scopus 로고    scopus 로고
    • Bacterial ribosomal subunit assembly is an antibiotic target
    • Champney W.S. Bacterial ribosomal subunit assembly is an antibiotic target. Curr. Top. Med. Chem. 3 (2003) 929-947
    • (2003) Curr. Top. Med. Chem. , vol.3 , pp. 929-947
    • Champney, W.S.1
  • 11
    • 59749083182 scopus 로고    scopus 로고
    • Erythromycin- and chloramphenicol-induced ribosomal assembly defects are secondary effects of protein synthesis inhibition
    • Siibak T., Peil L., Xiong L., Mankin A., Remme J., and Tenson T. Erythromycin- and chloramphenicol-induced ribosomal assembly defects are secondary effects of protein synthesis inhibition. Antimicrobial. Agents Chemother. 53 (2009) 563-571
    • (2009) Antimicrobial. Agents Chemother. , vol.53 , pp. 563-571
    • Siibak, T.1    Peil, L.2    Xiong, L.3    Mankin, A.4    Remme, J.5    Tenson, T.6
  • 12
    • 0028963496 scopus 로고
    • Erythromycin resistance by ribosome modification
    • Weisblum B. Erythromycin resistance by ribosome modification. Antimicrobial. Agents Chemother. 39 (1995) 577-585
    • (1995) Antimicrobial. Agents Chemother. , vol.39 , pp. 577-585
    • Weisblum, B.1
  • 13
    • 4544239063 scopus 로고    scopus 로고
    • The macrolide-bacterium interaction and its biological basis
    • Goldman R.C., and Scaglione F. The macrolide-bacterium interaction and its biological basis. Curr. Drug Targets Infect. Disord. 4 (2004) 241-260
    • (2004) Curr. Drug Targets Infect. Disord. , vol.4 , pp. 241-260
    • Goldman, R.C.1    Scaglione, F.2
  • 14
    • 0035160878 scopus 로고    scopus 로고
    • Macrolide resistance conferred by base substitutions in 23S rRNA
    • Vester B., and Douthwaite S. Macrolide resistance conferred by base substitutions in 23S rRNA. Antimicrobial. Agents Chemother. 45 (2001) 1-12
    • (2001) Antimicrobial. Agents Chemother. , vol.45 , pp. 1-12
    • Vester, B.1    Douthwaite, S.2
  • 15
    • 35748981771 scopus 로고    scopus 로고
    • Novel mutations in ribosomal proteins L4 and L22 that confer erythromycin resistance in Escherichia coli
    • Zaman S., Fitzpatrick M., Lindahl L., and Zengel J. Novel mutations in ribosomal proteins L4 and L22 that confer erythromycin resistance in Escherichia coli. Mol. Microbiol. 66 (2007) 1039-1050
    • (2007) Mol. Microbiol. , vol.66 , pp. 1039-1050
    • Zaman, S.1    Fitzpatrick, M.2    Lindahl, L.3    Zengel, J.4
  • 16
    • 59149098644 scopus 로고    scopus 로고
    • Recombineering reveals a diverse collection of ribosomal proteins L4 and L22 that confer resistance to macrolide antibiotics
    • Diner E.J., and Hayes C.S. Recombineering reveals a diverse collection of ribosomal proteins L4 and L22 that confer resistance to macrolide antibiotics. J. Mol. Biol. 386 (2009) 300-315
    • (2009) J. Mol. Biol. , vol.386 , pp. 300-315
    • Diner, E.J.1    Hayes, C.S.2
  • 17
    • 62649162761 scopus 로고    scopus 로고
    • Erythromycin resistance by L4/L22 mutations and resistance masking by drug efflux pump deficiency
    • Lovmar M., Nilsson K., Lukk E., Vimberg V., Tenson T., and Ehrenberg M. Erythromycin resistance by L4/L22 mutations and resistance masking by drug efflux pump deficiency. Embo J. 28 (2009) 736-744
    • (2009) Embo J. , vol.28 , pp. 736-744
    • Lovmar, M.1    Nilsson, K.2    Lukk, E.3    Vimberg, V.4    Tenson, T.5    Ehrenberg, M.6
  • 18
    • 0029953161 scopus 로고    scopus 로고
    • A functional peptide encoded in the Escherichia coli 23S rRNA
    • Tenson T., DeBlasio A., and Mankin A. A functional peptide encoded in the Escherichia coli 23S rRNA. Proc. Natl. Acad. Sci. U.S.A. 93 (1996) 5641-5646
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 5641-5646
    • Tenson, T.1    DeBlasio, A.2    Mankin, A.3
  • 19
    • 0030748654 scopus 로고    scopus 로고
    • Erythromycin resistance peptides selected from random peptide libraries
    • Tenson T., Xiong L., Kloss P., and Mankin A.S. Erythromycin resistance peptides selected from random peptide libraries. J. Biol. Chem. 272 (1997) 17425-17430
    • (1997) J. Biol. Chem. , vol.272 , pp. 17425-17430
    • Tenson, T.1    Xiong, L.2    Kloss, P.3    Mankin, A.S.4
  • 20
    • 0032493758 scopus 로고    scopus 로고
    • Ketolide resistance conferred by short peptides
    • Tripathi S., Kloss P.S., and Mankin A.S. Ketolide resistance conferred by short peptides. J. Biol. Chem. 273 (1998) 20073-20077
    • (1998) J. Biol. Chem. , vol.273 , pp. 20073-20077
    • Tripathi, S.1    Kloss, P.S.2    Mankin, A.S.3
  • 21
    • 6344275448 scopus 로고    scopus 로고
    • Peptide-mediated macrolide resistance reveals possible specific interactions in the nascent peptide exit tunnel
    • Vimberg V., Xiong L., Bailey M., Tenson T., and Mankin A. Peptide-mediated macrolide resistance reveals possible specific interactions in the nascent peptide exit tunnel. Mol. Microbiol. 54 (2004) 376-385
    • (2004) Mol. Microbiol. , vol.54 , pp. 376-385
    • Vimberg, V.1    Xiong, L.2    Bailey, M.3    Tenson, T.4    Mankin, A.5
  • 22
    • 0034817784 scopus 로고    scopus 로고
    • Short peptides conferring resistance to macrolide antibiotics
    • Tenson T., and Mankin A.S. Short peptides conferring resistance to macrolide antibiotics. Peptides 22 (2001) 1661-1668
    • (2001) Peptides , vol.22 , pp. 1661-1668
    • Tenson, T.1    Mankin, A.S.2
  • 24
    • 0018498843 scopus 로고
    • Nucleoside triphosphate regeneration decreases the frequency of translation errors
    • Jelenc P.C., and Kurland C.G. Nucleoside triphosphate regeneration decreases the frequency of translation errors. Proc. Natl. Acad. Sci. U.S.A. 76 (1979) 3174-3178
    • (1979) Proc. Natl. Acad. Sci. U.S.A. , vol.76 , pp. 3174-3178
    • Jelenc, P.C.1    Kurland, C.G.2
  • 25
    • 2342547059 scopus 로고    scopus 로고
    • Ribosome formation from subunits studied by stopped-flow and Rayleigh light scattering
    • Antoun A., Pavlov M.Y., Tenson T., and Ehrenberg M.M. Ribosome formation from subunits studied by stopped-flow and Rayleigh light scattering. Biol. Proced Online 6 (2004) 35-54
    • (2004) Biol. Proced Online , vol.6 , pp. 35-54
    • Antoun, A.1    Pavlov, M.Y.2    Tenson, T.3    Ehrenberg, M.M.4
  • 26
    • 0029873397 scopus 로고    scopus 로고
    • Rate of translation of natural mRNAs in an optimized in vitro system
    • Pavlov M.Y., and Ehrenberg M. Rate of translation of natural mRNAs in an optimized in vitro system. Arch. Biochem. Biophys. 328 (1996) 9-16
    • (1996) Arch. Biochem. Biophys. , vol.328 , pp. 9-16
    • Pavlov, M.Y.1    Ehrenberg, M.2
  • 27
    • 0030949960 scopus 로고    scopus 로고
    • Release factor RF3 in E. coli accelerates the dissociation of release factors RF1 and RF2 from the ribosome in a GTP-dependent manner
    • Freistroffer D.V., Pavlov M.Y., MacDougall J., Buckingham R.H., and Ehrenberg M. Release factor RF3 in E. coli accelerates the dissociation of release factors RF1 and RF2 from the ribosome in a GTP-dependent manner. Embo J. 16 (1997) 4126-4133
    • (1997) Embo J. , vol.16 , pp. 4126-4133
    • Freistroffer, D.V.1    Pavlov, M.Y.2    MacDougall, J.3    Buckingham, R.H.4    Ehrenberg, M.5
  • 28
    • 0030787025 scopus 로고    scopus 로고
    • Purification of active Escherichia coli ribosome recycling factor (RRF) from an osmo-regulated expression system
    • MacDougall J., Holst-Hansen P., Mortensen K.K., Freistroffer D.V., Pavlov M.Y., Ehrenberg M., et al. Purification of active Escherichia coli ribosome recycling factor (RRF) from an osmo-regulated expression system. Biochimie 79 (1997) 243-246
    • (1997) Biochimie , vol.79 , pp. 243-246
    • MacDougall, J.1    Holst-Hansen, P.2    Mortensen, K.K.3    Freistroffer, D.V.4    Pavlov, M.Y.5    Ehrenberg, M.6
  • 31
    • 0023447384 scopus 로고
    • Genetic and physical location of the Escherichia coli rap locus, which is essential for growth of bacteriophage lambda
    • Guarneros G., Machado G., Guzman P., and Garay E. Genetic and physical location of the Escherichia coli rap locus, which is essential for growth of bacteriophage lambda. J. Bacteriol. 169 (1987) 5188-5192
    • (1987) J. Bacteriol. , vol.169 , pp. 5188-5192
    • Guarneros, G.1    Machado, G.2    Guzman, P.3    Garay, E.4
  • 32
    • 0027169358 scopus 로고
    • Role of the 1-72 base pair in tRNAs for the activity of Escherichia coli peptidyl-tRNA hydrolase
    • Dutka S., Meinnel T., Lazennec C., Mechulam Y., and Blanquet S. Role of the 1-72 base pair in tRNAs for the activity of Escherichia coli peptidyl-tRNA hydrolase. Nucleic Acids Res. 21 (1993) 4025-4030
    • (1993) Nucleic Acids Res. , vol.21 , pp. 4025-4030
    • Dutka, S.1    Meinnel, T.2    Lazennec, C.3    Mechulam, Y.4    Blanquet, S.5
  • 33
    • 0030779476 scopus 로고    scopus 로고
    • Release factor RF3 abolishes competition between release factor RF1 and ribosome recycling factor (RRF) for a ribosome binding site
    • Pavlov M.Y., Freistroffer D.V., Heurgue-Hamard V., Buckingham R.H., and Ehrenberg M. Release factor RF3 abolishes competition between release factor RF1 and ribosome recycling factor (RRF) for a ribosome binding site. J. Mol. Biol. 273 (1997) 389-401
    • (1997) J. Mol. Biol. , vol.273 , pp. 389-401
    • Pavlov, M.Y.1    Freistroffer, D.V.2    Heurgue-Hamard, V.3    Buckingham, R.H.4    Ehrenberg, M.5
  • 34
    • 33745763700 scopus 로고    scopus 로고
    • How initiation factors tune the rate of initiation of protein synthesis in bacteria
    • Antoun A., Pavlov M.Y., Lovmar M., and Ehrenberg M. How initiation factors tune the rate of initiation of protein synthesis in bacteria. Embo J. 25 (2006) 2539-2550
    • (2006) Embo J. , vol.25 , pp. 2539-2550
    • Antoun, A.1    Pavlov, M.Y.2    Lovmar, M.3    Ehrenberg, M.4
  • 36
    • 0036810254 scopus 로고    scopus 로고
    • Release of peptide promoted by the GGQ motif of class 1 release factors regulates the GTPase activity of RF3
    • Zavialov A.V., Mora L., Buckingham R.H., and Ehrenberg M. Release of peptide promoted by the GGQ motif of class 1 release factors regulates the GTPase activity of RF3. Mol. Cell 10 (2002) 789-798
    • (2002) Mol. Cell , vol.10 , pp. 789-798
    • Zavialov, A.V.1    Mora, L.2    Buckingham, R.H.3    Ehrenberg, M.4
  • 37
    • 0033063428 scopus 로고    scopus 로고
    • Novel roles for classical factors at the interface between translation termination and initiation
    • Karimi R., Pavlov M.Y., Buckingham R.H., and Ehrenberg M. Novel roles for classical factors at the interface between translation termination and initiation. Mol. Cell 3 (1999) 601-609
    • (1999) Mol. Cell , vol.3 , pp. 601-609
    • Karimi, R.1    Pavlov, M.Y.2    Buckingham, R.H.3    Ehrenberg, M.4
  • 38
    • 33644891029 scopus 로고    scopus 로고
    • Highly expressed proteins have an increased frequency of alanine in the second amino acid position
    • Tats A., Remm M., and Tenson T. Highly expressed proteins have an increased frequency of alanine in the second amino acid position. BMC Genomics 7 (2006) 28
    • (2006) BMC Genomics , vol.7 , pp. 28
    • Tats, A.1    Remm, M.2    Tenson, T.3
  • 39
    • 47049098691 scopus 로고    scopus 로고
    • Complementary roles of initiation factor 1 and ribosome recycling factor in 70S ribosome splitting
    • Pavlov M.Y., Antoun A., Lovmar M., and Ehrenberg M. Complementary roles of initiation factor 1 and ribosome recycling factor in 70S ribosome splitting. Embo J. 27 (2008) 1706-1717
    • (2008) Embo J. , vol.27 , pp. 1706-1717
    • Pavlov, M.Y.1    Antoun, A.2    Lovmar, M.3    Ehrenberg, M.4


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