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PMID: 6195156 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Site of action of a ribosomal RNA methylase responsible for resistance to erythromycin and other antibiotics.

The Journal of biological chemistry ·Vol. 258 ·No. 20 ·1983-10-25 ·Pages 12702-6

Skinner R, Cundliffe E, Schmidt FJ

Abstract

The enzyme which confers resistance to erythromycin in the producing organism Streptomyces erythraeus dimethylates a single adenine residue in Bacillus stearothermophilus 23 S rRNA. This corresponds to residue Ade 2058 in Escherichia coli 23 S RNA. The methylase responsible for resistance to macrolides, lincomycin, and streptogramin B-related antibiotics in Staphylococcus aureus also acts at this site.

MeSH Terms

Anti-Bacterial Agents/toxicity Base Sequence Drug Resistance Erythromycin/toxicity Kinetics Methyltransferases/metabolism Nucleic Acid Conformation RNA, Bacterial RNA, Ribosomal Species Specificity Streptomyces/enzymology Substrate Specificity

Chemicals

Anti-Bacterial Agents RNA, Bacterial RNA, Ribosomal Erythromycin Methyltransferases rRNA (adenosine-O-2'-)methyltransferase

Authors & Affiliations

3 authors, click to expand affiliations / ORCID

Skinner R

Cundliffe E

Schmidt F J

Article Info

Journal

The Journal of biological chemistry

Abbr.

J Biol Chem

ISSN

0021-9258

Published

1983-10-25

Pages

12702-6

Language

English

Region

United States

NLM ID

2985121R

Subset

Grants

NIGMS NIH HHS · GM 26756 · United States

External Links

PubMed source View journal details

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Site of action of a ribosomal RNA methylase responsible for resistance to erythromycin and other antibiotics.

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