Inhibition of protein synthesis stabilizes histone mRNA

Journal Article · Mon Oct 01 04:00:00 EDT 1984 · Mol. Cell. Biol.; (United States)

DOI:https://doi.org/10.1128/MCB.4.10.2082· OSTI ID:5880712

Stimac, E; Groppi, Jr, V E; Coffino, P

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 > 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.

• Research Organization: Departments of Microbiology and Immunology, Pharmacology, and Medicine, Univ. of California, San Francisco, CA 94143
• OSTI ID: 5880712
• Journal Information: Mol. Cell. Biol.; (United States), Journal Name: Mol. Cell. Biol.; (United States) Vol. 4:10; ISSN MCEBD
• Country of Publication: United States
• Language: English

Related Subjects

550200* -- Biochemistry
59 BASIC BIOLOGICAL SCIENCES
ANTI-INFECTIVE AGENTS
ANTIBIOTICS
BIOLOGICAL PATHWAYS
CELL CULTURES
CHEMICAL PROPERTIES
CYCLOHEXIMIDE
DRUGS
ENZYME ACTIVITY
FUNGICIDES
GENE REGULATION
GENE REPRESSORS
HALF-LIFE
HISTONES
LABELLING
MESSENGER-RNA
METABOLISM
NUCLEIC ACIDS
NUCLEOPROTEINS
ORGANIC COMPOUNDS
PESTICIDES
PROTEINS
RNA
STRUCTURE-ACTIVITY RELATIONSHIPS
TOXICITY
TRANSCRIPTION