ADP-ribosylation as an intermediate step in inactivation of rifampin by a mycobacterial gene

被引:36
作者
Quan, S
Imai, T
Mikami, Y
Yazawa, K
Dabbs, ER
Morisaki, N
Iwasaki, S
Hashimoto, Y
Furihata, K
机构
[1] Chiba Univ, Pathogen Fungi & Microbial Toxicoses Res Ctr, Chuo Ku, Chiba 2608673, Japan
[2] Univ Tokyo, Inst Mol & Cellular Biosci, Bunkyo Ku, Tokyo 113, Japan
[3] Univ Tokyo, Dept Agr Chem, Bunkyo Ku, Tokyo 113, Japan
[4] Univ Witwatersrand, Dept Genet, ZA-2050 Johannesburg, South Africa
关键词
D O I
10.1128/AAC.43.1.181
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Mycobacterium smegmatis DSM43756 inactivates rifampin, and the inactivated antibiotic product recovered from culture medium was ribosylated on the 23-OH group. To study this process, the gene responsible for the inactivation was expressed at high levels by the lac promoter in Escherichia coli conferring resistance to >500 mu g of antibiotic per mi. Cell homogenates generated a novel derivative designated RIP-TAs; in this study, we determined that RIP-TAs is 23 (O-ADP-ribosyl)rifampin. Our results indicated that RIP-TAs is an intermediate in the pathway leading to ribosylated rifampin and that the previously characterized gene encodes a mono(ADP-ribosyl)transferase which, however, shows no sequence similarity to other enzymes of this class.
引用
收藏
页码:181 / 184
页数:4
相关论文
共 25 条
[1]   C-13 NUCLEAR-MAGNETIC-RESONANCE STUDY OF ENZYME COFACTOR FLAVIN-ADENINE DINUCLEOTIDE [J].
BREITMAIER, E ;
VOELTER, W .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1972, 31 (02) :234-+
[2]   NAD BINDING-SITE OF DIPHTHERIA-TOXIN - IDENTIFICATION OF A RESIDUE WITHIN THE NICOTINAMIDE SUBSITE BY PHOTOCHEMICAL MODIFICATION WITH NAD [J].
CARROLL, SF ;
COLLIER, RJ .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA-BIOLOGICAL SCIENCES, 1984, 81 (11) :3307-3311
[3]   RIBOSYLATION BY MYCOBACTERIAL STRAINS AS A NEW MECHANISM OF RIFAMPIN INACTIVATION [J].
DABBS, ER ;
YAZAWA, K ;
MIKAMI, Y ;
MIYAJI, M ;
MORISAKI, N ;
IWASAKI, S ;
FURIHATA, K .
ANTIMICROBIAL AGENTS AND CHEMOTHERAPY, 1995, 39 (04) :1007-1009
[4]   HYDROLYSIS OF ADENOSINE DIPHOSPHATE RIBOSE BY A SPECIFIC PHOSPHOHYDROLASE OF RABBIT-MUSCLE EXTRACTS [J].
DOHERTY, MD ;
MORRISON, JF .
BIOCHIMICA ET BIOPHYSICA ACTA, 1962, 65 (02) :364-&
[5]   Three conserved consensus sequences identify the NAD-binding site of ADP-ribosylating enzymes, expressed by eukaryotes, bacteria and T-even bacteriophages [J].
Domenighini, M ;
Rappuoli, R .
MOLECULAR MICROBIOLOGY, 1996, 21 (04) :667-674
[6]   EVALUATION OF THE RPOB GENE IN RIFAMPICIN-SUSCEPTIBLE AND RIFAMPICIN-RESISTANT MYCOBACTERIUM-AVIUM AND MYCOBACTERIUM-INTRACELLULARE [J].
GUERRERO, C ;
STOCKMAN, L ;
MARCHESI, F ;
BODMER, T ;
ROBERTS, GD ;
TELENTI, A .
JOURNAL OF ANTIMICROBIAL CHEMOTHERAPY, 1994, 33 (03) :661-663
[7]   SEQUENCE AND ANALYSIS OF THE RPOB GENE OF MYCOBACTERIUM-SMEGMATIS [J].
HETHERINGTON, SV ;
WATSON, AS ;
PATRICK, CC .
ANTIMICROBIAL AGENTS AND CHEMOTHERAPY, 1995, 39 (09) :2164-2166
[8]   MOLECULAR-BASIS OF RIFAMPIN RESISTANCE IN MYCOBACTERIUM-LEPRAE [J].
HONORE, N ;
COLE, ST .
ANTIMICROBIAL AGENTS AND CHEMOTHERAPY, 1993, 37 (03) :414-418
[9]   THE ADP-RIBOSYLTRANSFERASES (GPALT) OF BACTERIOPHAGES T2, T4, AND T6 - SEQUENCING OF THE GENES AND COMPARISON OF THEIR PRODUCTS [J].
KOCH, T ;
RUGER, W .
VIROLOGY, 1994, 203 (02) :294-298
[10]  
LOWERY RG, 1990, ADP RIBOSYLATING TOX, P459