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PMID: 6209555 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Inhibition of protein synthesis stabilizes histone mRNA.

Molecular and cellular biology ·Vol. 4 ·No. 10 ·1984-10-00 ·Pages 2082-90

Stimac E, Groppi VE, Coffino P

Abstract

The inhibition of protein synthesis in exponentially growing S49 cells leads to a specific fivefold increase in histone mRNA in 30 min. The rate of transcription of histone mRNA, measured in intact or digitonin-permeabilized cells, is increased slightly, if at all, by cycloheximide inhibition of protein synthesis. Both approach-to-equilibrium labeling and pulse-chase experiments show that cycloheximide prolongs histone mRNA half-life from approximately 30 min to greater than 2 h. Histone mRNA made before the addition of cycloheximide becomes stable after the inhibition of protein synthesis, whereas removal of the inhibitor is followed by rapid degradation of histone mRNA. This suggests that the increased stability of histone mRNA during inhibition of protein synthesis results not from alteration of the structure of the mRNA, but from the loss of an activity in the cell which regulates histone mRNA turnover.

MeSH Terms
Actins/genetics Animals Cell Line Cycloheximide/pharmacology DNA/metabolism Electrophoresis, Polyacrylamide Gel Histones/genetics Lymphoma/metabolism Mice Nucleic Acid Hybridization Poly A/metabolism Protein Biosynthesis RNA/metabolism RNA, Messenger/metabolism Transcription, Genetic
Chemicals
Actins Histones RNA, Messenger Poly A RNA DNA Cycloheximide
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Stimac E
Groppi V E
Coffino P
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Article Info
Journal
Molecular and cellular biology
Abbr.
Mol Cell Biol
ISSN
0270-7306
Published
1984-10-00
Pages
2082-90
Language
English
Region
United States
NLM ID
8109087
PMCID
PMC369025
Subset
IM
Grants
NCI NIH HHS · CA09043 · United States
NCI NIH HHS · CA29048 · United States
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