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PMID: 770427 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Effect of arginine on the stability and size of argECBH messenger ribonucleic acid in Escherichia coli.

Journal of bacteriology ·Vol. 126 ·No. 1 ·1976-04-00 ·Pages 365-76

Krzyzek RA, Rogers P

Abstract

The chemical stability of argECBH messenger ribonucleic acid (mRNA) produced by Escherichia coli was found to be unaltered during steady-state repression by arginine. During extreme arginine deprivation, the increase in argECBH mRNA stability was related to general effects of amino acid starvation on mRNA stability. Thus a mechanism whereby argECBH gene expression is regulated by altering the decay rate of this mRNA is not consistent with our data. Sucrose gradient analysis followed by hybridization revealed that both heavy (14S) and light (8S) components of argECBH mRNA were produced by cells of E. coli K-12 grown without arginine, whereas predominantly light (8S) mRNA was produced by cells grown with arginine. A functional argR gene and the EC portion of the argECBH cluster were found essential for the arginine restriction of heavy-mRNA production. Experiments suggest that light argECBH mRNA did not arise from heavy message, and 8u% of both light and heavy mRNA was found bound to ribosomes. The data appear most consistent with the notion that a second site of control by arginine regulates the amounts of light and heavy arginine mRNA in the cell either by early termination of transcription or by endonucleolytic processing. Consideration of these data in conjunction with those of the accompanying report (Krzyzek and Rogers, 1976) permits the tentative conclusion that light argECBH mRNA is not translated into active enzymes and is thus responsible for the discrepancy between the high content of hybridizable mRNA and low rates of enzyme synthesis found during arginine repression.

MeSH Terms
Amidohydrolases/biosynthesis Arginine/metabolism,pharmacology Argininosuccinate Lyase/biosynthesis Enzyme Repression Escherichia coli/metabolism Lyases/biosynthesis Operon Polyribosomes/metabolism Protein Biosynthesis RNA, Bacterial/biosynthesis,metabolism RNA, Messenger/biosynthesis,metabolism
Chemicals
RNA, Bacterial RNA, Messenger Arginine Amidohydrolases Lyases Argininosuccinate Lyase
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Krzyzek R A
Rogers P
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29 references, click to expand
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
Published
1976-04-00
Pages
365-76
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC233293
Subset
IM
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