메뉴 건너뛰기




Volumn 4, Issue 1, 2011, Pages 1-10

Insights into the Chloramphenicol Inhibition Effect on Peptidyl Transferase Activity, Using Two New Analogs of the Drug

Author keywords

23S rRNA; Chloramphenicol; Chloramphenicol derivatives; Peptide exit tunnel; Peptidyl transferase; Puromycin reaction; Ribosomal A site; Ribosome; Slow binding inhibitors

Indexed keywords

CHLORAMPHENICOL; NUCLEOTIDE; PEPTIDYLTRANSFERASE;

EID: 80053480606     PISSN: None     EISSN: 18749402     Source Type: Journal    
DOI: 10.2174/1874940201104010001     Document Type: Article
Times cited : (14)

References (34)
  • 1
    • 49649099086 scopus 로고    scopus 로고
    • Chloramphenicol induces abnormal differentiation and inhibits apoptosis in activated T cells
    • Yuan ZR, Shi Y. Chloramphenicol induces abnormal differentiation and inhibits apoptosis in activated T cells. Cancer Res 2008; 68: 4875-81.
    • (2008) Cancer Res , vol.68 , pp. 4875-4881
    • Yuan, Z.R.1    Shi, Y.2
  • 2
    • 34547354966 scopus 로고    scopus 로고
    • Resistance to ocular antibiotics: An overview
    • Brown L. Resistance to ocular antibiotics: an overview. Clin Exp Optom 2007; 90: 258-62.
    • (2007) Clin Exp Optom , vol.90 , pp. 258-262
    • Brown, L.1
  • 3
    • 0014702171 scopus 로고
    • Studies on the formation of transfer ribonucleic acidribosome complexes. VII. Survey of the effect of antibiotics of Nacetyl- phenylalanyl-puromycin formation: Possible mechanism of chloramphenicol action
    • Pestka S. Studies on the formation of transfer ribonucleic acidribosome complexes. VII. Survey of the effect of antibiotics of Nacetyl- phenylalanyl-puromycin formation: possible mechanism of chloramphenicol action. Arch Biochem Biophys 1970; 136: 80-8.
    • (1970) Arch Biochem Biophys , vol.136 , pp. 80-88
    • Pestka, S.1
  • 4
    • 0001883257 scopus 로고
    • Kinetic studies of peptide bond formation. Effect of chloramphenicol
    • Fernandez-Muñoz R, Vazquez D. Kinetic studies of peptide bond formation. Effect of chloramphenicol. Mol Biol Rep 1973; 1: 75-9.
    • (1973) Mol Biol Rep , vol.1 , pp. 75-79
    • Fernandez-Muñoz, R.1    Vazquez, D.2
  • 5
    • 0023120568 scopus 로고
    • Inhibition of ribosomal peptidyltransferase by chloramphenicol
    • Kinetic studies
    • Drainas D, Kalpaxis DL, Coutsogeorgopoulos C. Inhibition of ribosomal peptidyltransferase by chloramphenicol. Kinetic studies. Eur J Biochem 1987; 164: 53-8.
    • (1987) Eur J Biochem , vol.164 , pp. 53-58
    • Drainas, D.1    Kalpaxis, D.L.2    Coutsogeorgopoulos, C.3
  • 6
    • 0344875468 scopus 로고    scopus 로고
    • Effect of polyamines on the inhibition of peptidyltransferase by antibiotics: Revisiting the mechanism of chloramphenicol action
    • Xaplanteri MA, Andreou A, Dinos GP, Kalpaxis DL. Effect of polyamines on the inhibition of peptidyltransferase by antibiotics: revisiting the mechanism of chloramphenicol action. Nucleic Acids Res 2003; 31: 5074-83.
    • (2003) Nucleic Acids Res , vol.31 , pp. 5074-5083
    • Xaplanteri, M.A.1    Andreou, A.2    Dinos, G.P.3    Kalpaxis, D.L.4
  • 7
    • 0025151914 scopus 로고
    • Partial release of AcPhe-Phe-tRNA from ribosomes during poly(U)-dependent poly(Phe) synthesis and the effects of chloramphenicol
    • Rheinberger HJ, Nierhaus KH. Partial release of AcPhe-Phe-tRNA from ribosomes during poly(U)-dependent poly(Phe) synthesis and the effects of chloramphenicol. Eur J Biochem 1990; 193: 643-50.
    • (1990) Eur J Biochem , vol.193 , pp. 643-650
    • Rheinberger, H.J.1    Nierhaus, K.H.2
  • 8
    • 0030904329 scopus 로고    scopus 로고
    • Movement of the 3'-end of tRNA through the peptidyltransferase centre and its inhibition by antibiotics
    • Kirillov S, Porse BT, Vester B, Woolley P, Garrett RA. Movement of the 3'-end of tRNA through the peptidyltransferase centre and its inhibition by antibiotics. FEBS Lett 1997; 406: 223-33.
    • (1997) FEBS Lett , vol.406 , pp. 223-233
    • Kirillov, S.1    Porse, B.T.2    Vester, B.3    Woolley, P.4    Garrett, R.A.5
  • 10
    • 0037245660 scopus 로고    scopus 로고
    • The critical role of the universally conserved A2602 of 23S ribosomal RNA in the release of the nascent peptide during translation termination
    • Polacek N, Gomez MJ, Ito K, Xiong L, Nakamura Y, Mankin A. The critical role of the universally conserved A2602 of 23S ribosomal RNA in the release of the nascent peptide during translation termination. Mol Cell 2003; 11: 103-12.
    • (2003) Mol Cell , vol.11 , pp. 103-112
    • Polacek, N.1    Gomez, M.J.2    Ito, K.3    Xiong, L.4    Nakamura, Y.5    Mankin, A.6
  • 11
    • 0015220211 scopus 로고
    • Substrate and antibiotic binding sites at the peptidyl-transferase centre of Escherichia coli ribosomes. Studies on the chloramphenicol, lincomycin and erythromycin sites
    • Fernandez-Munoz R, Monro RE, Torres-Pinedo R, Vazquez D. Substrate and antibiotic binding sites at the peptidyl-transferase centre of Escherichia coli ribosomes. Studies on the chloramphenicol, lincomycin and erythromycin sites. Eur J Biochem 1971; 23: 185-93.
    • (1971) Eur J Biochem , vol.23 , pp. 185-193
    • Fernandez-Munoz, R.1    Monro, R.E.2    Torres-Pinedo, R.3    Vazquez, D.4
  • 12
    • 0035950132 scopus 로고    scopus 로고
    • Structural basis for the interaction of antibiotics with the peptidyl transferase centre in eubacteria
    • Schlünzen F, Zarivach R, Harms J, et al. Structural basis for the interaction of antibiotics with the peptidyl transferase centre in eubacteria. Nature 2001; 413: 814-21.
    • (2001) Nature , vol.413 , pp. 814-821
    • Schlünzen, F.1    Zarivach, R.2    Harms, J.3
  • 13
    • 78049250815 scopus 로고    scopus 로고
    • Revisiting the structures of several antibiotics bound to the bacterial ribosome
    • Bulkley D, Innis CA, Blaha G, Steitz TA. Revisiting the structures of several antibiotics bound to the bacterial ribosome. Proc Natl Acad Sci USA 2010; 107: 17158-63.
    • (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
  • 14
    • 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. 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: 17152-57.
    • (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
  • 15
    • 0032605633 scopus 로고    scopus 로고
    • Mutational analysis of 23S ribosomal RNA structure and function in Escherichia coli
    • Triman KL. Mutational analysis of 23S ribosomal RNA structure and function in Escherichia coli. Adv Genet 1999; 41: 157-95.
    • (1999) Adv Genet , vol.41 , pp. 157-195
    • Triman, K.L.1
  • 17
    • 0023604799 scopus 로고
    • Chloramphenicol, erythromycin, carbomycin and vernamycin B protect overlapping sites in the peptidyl transferase region of 23S ribosomal RNA
    • Moazed D, Noller HF. Chloramphenicol, erythromycin, carbomycin and vernamycin B protect overlapping sites in the peptidyl transferase region of 23S ribosomal RNA. Biochimie 1987; 69: 879-84.
    • (1987) Biochimie , vol.69 , pp. 879-884
    • Moazed, D.1    Noller, H.F.2
  • 18
    • 0028924641 scopus 로고
    • Fine structure of the peptidyl-transferase centre on 23S-like rRNAs deduced from chemical probing of antibiotic-ribosome complexes
    • Rodriguez-Fonseca C, Amils R, Garrett RA. Fine structure of the peptidyl-transferase centre on 23S-like rRNAs deduced from chemical probing of antibiotic-ribosome complexes. J Mol Biol 1995; 247: 224-35.
    • (1995) J Mol Biol , vol.247 , pp. 224-235
    • Rodriguez-Fonseca, C.1    Amils, R.2    Garrett, R.A.3
  • 19
    • 0036342198 scopus 로고    scopus 로고
    • The structures of four macrolide antibiotics bound to the large ribosomal subunit
    • Hansen JL, Ippolito JA, Ban N, Nissen P, Moore PB, Steitz TA. The structures of four macrolide antibiotics bound to the large ribosomal subunit. Mol Cell 2002; 10: 117-28.
    • (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
  • 20
    • 0346252659 scopus 로고    scopus 로고
    • A conserved chloramphenicol binding site at the entrance to the ribosomal peptide exit tunnel
    • Long KS, Porse BT. A conserved chloramphenicol binding site at the entrance to the ribosomal peptide exit tunnel. Nucleic Acids Res 2003; 31: 7208-15.
    • (2003) Nucleic Acids Res , vol.31 , pp. 7208-7215
    • Long, K.S.1    Porse, B.T.2
  • 21
    • 0004526983 scopus 로고
    • Chloramphenicol
    • In: Hahn FE, Ed, New York: Springer-Verlag
    • Pongs O. Chloramphenicol. In: Hahn FE, Ed. Antibiotics, New York: Springer-Verlag 1979; pp. 26-42.
    • (1979) Antibiotics , pp. 26-42
    • Pongs, O.1
  • 22
    • 33947488929 scopus 로고
    • The use of esters of N-hydroxysuccinimide in peptide synthesis
    • Anderson GW, Zimmerman JE, Callahan FM. The use of esters of N-hydroxysuccinimide in peptide synthesis. J Am Chem Soc 1964; 86: 1839-42.
    • (1964) J Am Chem Soc , vol.86 , pp. 1839-1842
    • Anderson, G.W.1    Zimmerman, J.E.2    Callahan, F.M.3
  • 23
    • 0027145095 scopus 로고
    • Aminoacyl analogs of chloramphenicol: Examination of the kinetics of inhibition of peptide bond formation
    • Drainas D, Mamos P, Coutsogeorgopoulos C. Aminoacyl analogs of chloramphenicol: examination of the kinetics of inhibition of peptide bond formation. J Med Chem 1993; 36: 3542-45.
    • (1993) J Med Chem , vol.36 , pp. 3542-3545
    • Drainas, D.1    Mamos, P.2    Coutsogeorgopoulos, C.3
  • 24
    • 1642564526 scopus 로고    scopus 로고
    • Dissecting the ribosomal inhibition mechanisms of edeine and pactamycin: The universally conserved residues G693 and C795 regulate P-site RNA binding
    • Dinos G, Wilson DN, Teraoka Y, et al. Dissecting the ribosomal inhibition mechanisms of edeine and pactamycin: the universally conserved residues G693 and C795 regulate P-site RNA binding. Mol Cell 2004; 13:113-24.
    • (2004) Mol Cell , vol.13 , pp. 113-124
    • Dinos, G.1    Wilson, D.N.2    Teraoka, Y.3
  • 25
    • 41949120352 scopus 로고    scopus 로고
    • Stepwise binding of tylosin and erythromycin to Escherichia coli ribosomes, characterized by kinetic and footprinting analysis
    • Petropoulos AD, Kouvela EC, Dinos GP, Kalpaxis DL. Stepwise binding of tylosin and erythromycin to Escherichia coli ribosomes, characterized by kinetic and footprinting analysis. J Biol Chem 2008; 283: 4756-65.
    • (2008) J Biol Chem , vol.283 , pp. 4756-4765
    • Petropoulos, A.D.1    Kouvela, E.C.2    Dinos, G.P.3    Kalpaxis, D.L.4
  • 26
    • 0024241761 scopus 로고
    • Structural analysis of RNA using chemical and enzymatic probing monitored by primer extension
    • Stern S, Moazed D, Noller HF. Structural analysis of RNA using chemical and enzymatic probing monitored by primer extension. Methods Enzymol 1988; 164: 481-89.
    • (1988) Methods Enzymol , vol.164 , pp. 481-489
    • Stern, S.1    Moazed, D.2    Noller, H.F.3
  • 27
    • 0023728105 scopus 로고
    • The behavior and significance of slowbinding enzyme inhibitors
    • Morrison JF, Walsh CT. The behavior and significance of slowbinding enzyme inhibitors. Adv Enzymol Relat Areas Mol Biol 1988; 61: 201-301.
    • (1988) Adv Enzymol Relat Areas Mol Biol , vol.61 , pp. 201-301
    • Morrison, J.F.1    Walsh, C.T.2
  • 29
    • 13844280352 scopus 로고    scopus 로고
    • A time-resolved investigation of ribosomal subunit association
    • Hennelly SP, Antoun A, Ehrenberg M, et al. A time-resolved investigation of ribosomal subunit association. J Mol Biol 2005; 346: 1243-58.
    • (2005) J Mol Biol , vol.346 , pp. 1243-1258
    • Hennelly, S.P.1    Antoun, A.2    Ehrenberg, M.3
  • 30
    • 0002476512 scopus 로고
    • Structural map of 23S rRNA
    • In: Hill WE, Moore PB, Dahlberg A, Schlessinger D, Garrett RA, Warner JB, Eds, Washington: Am Soc Microbiol
    • Egebjerg J, Larsen N, Garrett RA. Structural map of 23S rRNA. In: Hill WE, Moore PB, Dahlberg A, Schlessinger D, Garrett RA, Warner JB, Eds. The ribosome: structure, function and evolution. Washington: Am Soc Microbiol 1990; pp. 168-79.
    • (1990) The Ribosome: Structure, Function and Evolution , pp. 168-179
    • Egebjerg, J.1    Larsen, N.2    Garrett, R.A.3
  • 31
    • 23744453392 scopus 로고    scopus 로고
    • A new mechanism for chloramphenicol, florfenicol and clindamycin resistance: Methylation of 23S ribosomal RNA at A2503
    • Kehrenberg C, Schwarz S, Jacobsen L, Hansen LH, Vester B. A new mechanism for chloramphenicol, florfenicol and clindamycin resistance: methylation of 23S ribosomal RNA at A2503. Mol Microbiol 2005; 57: 1064-73.
    • (2005) Mol Microbiol , vol.57 , pp. 1064-1073
    • Kehrenberg, C.1    Schwarz, S.2    Jacobsen, L.3    Hansen, L.H.4    Vester, B.5
  • 34
    • 0031028280 scopus 로고    scopus 로고
    • Aminoacyl and peptidyl analogs of chloramphenicol as slow-binding inhibitors of ribosomal peptidyltransferase: A new approach for evaluating their potency
    • Michelinaki M, Mamos P, Coutsogeorgopoulos C, Kalpaxis DL. Aminoacyl and peptidyl analogs of chloramphenicol as slow-binding inhibitors of ribosomal peptidyltransferase: A new approach for evaluating their potency. Mol Pharmacol 1997; 51: 139-46.
    • (1997) Mol Pharmacol , vol.51 , pp. 139-146
    • Michelinaki, M.1    Mamos, P.2    Coutsogeorgopoulos, C.3    Kalpaxis, D.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.