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PMID: 4320462 Published · ppublish English Journal Article

Binding of adenosine 3':5'-cyclic phosphate to G factor of Escherichia coli, and its effects on GTPase, RNase V, and protein synthesis.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 66 ·No. 1 ·1970-05-00 ·Pages 146-52

Kuwano M, Schlessinger D

Abstract

Unique among adenine nucleotides tested by filter binding assays, 3':5'-cyclic AMP binds to the G translocation factor. Binding is dependent on the presence of GTP, and is inhibited by GDP, by the analog 5'-beta,gamma-methylene GTP, and by the antibiotic fusidic acid. The cAMP seems to be released during the ribosome-dependent translocation of charged tRNA catalyzed by G factor. Bound cAMP inhibits GTPase and ribosome-associated degradation of messenger RNA, but does not inhibit protein synthesis. cAMP might thereby regulate the ratio of productive to degradative transits of ribosomes on messenger RNA, and this may account for some part of its profound effect on levels of specific bacterial messenger RNA species.

MeSH Terms
Adenine Nucleotides/metabolism Bacterial Proteins/biosynthesis Chromosome Aberrations Cyclic AMP/metabolism Escherichia coli/metabolism Genetics, Microbial Guanine Nucleotides/metabolism,pharmacology Nucleotidases/metabolism Protein Binding RNA, Messenger/metabolism Ribonucleases/metabolism Ribosomes/metabolism
Chemicals
Adenine Nucleotides Bacterial Proteins Guanine Nucleotides RNA, Messenger Cyclic AMP Ribonucleases Nucleotidases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Kuwano M
Schlessinger D
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28 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.66.1.146
Published
1970-05-00
Pages
146-52
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC286100
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.66.1.146 PMC Full Text View journal details
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