ADP-Ribosylation as an Intermediate Step in Inactivation of Rifampin by a Mycobacterial Gene | Zendy

Selwyn Quan | Zendy; Tamae Imai | Zendy; Yuzuru Mikami | Zendy; Katsukiyo Yazawa | Zendy; Eric R. Dabbs | Zendy; Naoko Morisaki | Zendy; Shigeo Iwasaki | Zendy; Yuichi Hashimoto | Zendy; Kazuo Furihata | Zendy

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ADP-Ribosylation as an Intermediate Step in Inactivation of Rifampin by a Mycobacterial Gene

Author(s) -

Selwyn Quan,

Tamae Imai,

Yuzuru Mikami,

Katsukiyo Yazawa,

Eric R. Dabbs,

Naoko Morisaki,

Shigeo Iwasaki,

Yuichi Hashimoto,

Kazuo Furihata

Publication year - 1999

Publication title -

antimicrobial agents and chemotherapy

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.07

H-Index - 259

eISSN - 1070-6283

pISSN - 0066-4804

DOI - 10.1128/aac.43.1.181

Subject(s) - mycobacterium smegmatis , gene , escherichia coli , biology , gene product , microbiology and biotechnology , enzyme , transferase , antibiotics , biochemistry , gene expression , mycobacterium tuberculosis , medicine , tuberculosis , pathology

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 microg of antibiotic per ml. 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.

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