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PMID: 6806287 Published · ppublish English 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 conferring resistance to thiostrepton.

The Journal of biological chemistry ·Vol. 257 ·No. 14 ·1982-07-25 ·Pages 7915-7

Thompson J, Schmidt F, Cundliffe E

Abstract

A methylase enzyme, responsible for autoimmunity in the thiostrepton producer Streptomyces azureus, renders ribosomes completely resistant to thiostrepton. This RNA-pentose methylase modifies adenosine-1067 of Escherichia coli 23 S rRNA.

MeSH Terms
Adenosine Anti-Bacterial Agents/pharmacology Base Sequence Drug Resistance, Microbial Methyltransferases/metabolism Nucleic Acid Conformation RNA, Ribosomal Ribonuclease T1 Ribosomes/enzymology Streptomyces/enzymology Substrate Specificity Thiostrepton/pharmacology
Chemicals
Anti-Bacterial Agents RNA, Ribosomal Methyltransferases rRNA (adenosine-O-2'-)methyltransferase Ribonuclease T1 Thiostrepton Adenosine
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Thompson J
Schmidt F
Cundliffe E
Article Info
Journal
The Journal of biological chemistry
Abbr.
J Biol Chem
ISSN
0021-9258
Published
1982-07-25
Pages
7915-7
Language
English
Region
United States
NLM ID
2985121R
Subset
IM
Grants
NIGMS NIH HHS · GM 26756 · United States
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