PMID: 7543473Aug 1, 1995Paper

Substrate requirements for ErmC' methyltransferase activity

Journal of Bacteriology
P ZhongL Katz

Abstract

ErmC' is a methyltransferase that confers resistance to the macrolide-lincosamide-streptogramin B group of antibiotics by catalyzing the methylation of 23S rRNA at a specific adenine residue (A-2085 in Bacillus subtilis; A-2058 in Escherichia coli). The gene for ErmC' was cloned and expressed to a high level in E. coli, and the protein was purified to virtual homogeneity. Studies of substrate requirements of ErmC' have shown that a 262-nucleotide RNA fragment within domain V of B. subtilis 23S rRNA can be utilized efficiently as a substrate for methylation at A-2085. Kinetic studies of the monomethylation reaction showed that the apparent Km of this 262-nucleotide RNA oligonucleotide was 26-fold greater than the value determined for full-size and domain V 23S rRNA. In addition, the Vmax for this fragment also rose sevenfold. A model of RNA-ErmC' interaction involving multiple binding sites is proposed from the kinetic data presented.

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Citations

Nov 1, 1995·Biochemistry and Cell Biology = Biochimie Et Biologie Cellulaire·S DouthwalteB Vester
Nov 24, 1999·Microbial Drug Resistance : MDR : Mechanisms, Epidemiology, and Disease·P ZhongL Katz
Jul 5, 2018·Journal of Molecular Modeling·Katarzyna Kulczycka-MierzejewskaJoanna Trylska
Jun 24, 2020·Antimicrobial Agents and Chemotherapy·Hak Jin LeeHyung Jong Jin
Mar 7, 2018·MSphere·Yongjin LiuPaul D Straight
Apr 4, 2021·Antibiotics·Hak Jin LeeHyung Jong Jin
Sep 15, 1998·Journal of Molecular Biology·B VesterS Douthwaite
Aug 11, 2001·Drug Resistance Updates : Reviews and Commentaries in Antimicrobial and Anticancer Chemotherapy·Ping Zhong, Virginia D. Shortridge

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