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PMID: 4589896 Published · ppublish English Journal Article

The requirement for ribosomal proteins L7 and L12 in peptide-chain termination.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 71 ·No. 1 ·1974-01-00 ·Pages 89-92

Brot N, Tate WP, Caskey CT, Weissbach H

Abstract

Proteins L7 and L12 from 50S ribosomal subunits of Escherichia coli are required for peptidechain termination. This termination process is inhibited by thiostrepton. Since both thiostrepton-treated ribosomes and those depleted of L7 and L12 have a markedly reduced ability to form release factor.UA[(3)H]A.ribosome complexes, the binding of release factors to the ribosome appears to be the primary site of inhibition.

MeSH Terms
Anti-Bacterial Agents/pharmacology Bacterial Proteins/antagonists & inhibitors,metabolism Binding Sites Escherichia coli/metabolism Methionine/metabolism Peptide Chain Termination, Translational/drug effects Peptide Termination Factors Peptides/pharmacology RNA, Messenger/metabolism Ribosomes/drug effects,metabolism Tritium
Chemicals
Anti-Bacterial Agents Bacterial Proteins Peptide Termination Factors Peptides RNA, Messenger Tritium Methionine
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Brot N
Tate W P
Caskey C T
Weissbach H
References (36)
36 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.71.1.89
Published
1974-01-00
Pages
89-92
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC387938
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.71.1.89 PMC Full Text View journal details
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