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PMID: 4331558 Published · ppublish English Journal Article

Inhibition by siomycin and thiostrepton of both aminoacyl-tRNA and factor G binding to ribosomes.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 68 ·No. 8 ·1971-08-00 ·Pages 1796-800

Modolell J, Cabrer B, Parmeggiani A, Vazquez D

Abstract

Siomycin, a peptide antibiotic that interacts with the 50S ribosomal subunit and inhibits binding of factor G, is shown also to inhibit binding of aminoacyl-tRNA; however, it does not impair binding of fMet-tRNA and completion of the initiation complex. Moreover, unlike other inhibitors of aminoacyl-tRNA binding (tetracycline, sparsomycin, and streptogramin A), siomycin completely abolishes the GTPase activity associated with the binding of aminoacyl-tRNA catalyzed by factor T(u). A single-site interaction of siomycin appears to be responsible for its effect on both the binding of the aminoacyl-tRNA-T(u)-GTP complex and that of factor G.

MeSH Terms
Anti-Bacterial Agents/pharmacology Binding Sites Fusidic Acid/pharmacology Guanosine Triphosphate Hydrolysis Peptide Biosynthesis Peptide Chain Elongation, Translational Peptides/pharmacology Phosphoric Monoester Hydrolases/antagonists & inhibitors RNA, Transfer/antagonists & inhibitors,metabolism Ribosomes/drug effects,metabolism Tetracycline/pharmacology
Chemicals
Anti-Bacterial Agents Peptides Fusidic Acid Guanosine Triphosphate RNA, Transfer Phosphoric Monoester Hydrolases Tetracycline
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Modolell J
Cabrer B
Parmeggiani A
Vazquez D
References (29)
29 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.68.8.1796
Published
1971-08-00
Pages
1796-800
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC389295
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.68.8.1796 PMC Full Text View journal details
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