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PMID: 3561417 Published · ppublish English Journal Article Research Support, U.S. Gov't, P.H.S.

Initiation factor protein modifications and inhibition of protein synthesis.

Molecular and cellular biology ·Vol. 7 ·No. 3 ·1987-03-00 ·Pages 1293-5

Duncan RF, Hershey JW

Abstract

The protein covalent modification state of eucaryotic initiation factors eIF-2 and eIF-4B in HeLa cells was examined after they were exposed to a variety of conditions or treatments that regulate protein synthesis. A few factors (e.g., variant pH and sodium fluoride) altered the phosphorylation state of the initiation factor proteins, but the majority (hypertonic medium, ethanol, dimethyl sulfoxide sodium selenite, sodium azide, and colchicine) had no effect on either protein. While initiation factor phosphorylation may regulate protein synthesis in response to many physiological situations, other pathways can regulate protein synthesis under nonphysiological circumstances.

MeSH Terms
HeLa Cells/drug effects,metabolism Humans Hydrogen-Ion Concentration Peptide Initiation Factors/metabolism Phosphorylation Protein Biosynthesis Sodium Fluoride/pharmacology
Chemicals
Peptide Initiation Factors Sodium Fluoride
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Duncan R F
Hershey J W
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26 references, click to expand
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Article Info
Journal
Molecular and cellular biology
Abbr.
Mol Cell Biol
ISSN
0270-7306
DOI
10.1128/mcb.7.3.1293-1295.1987
Published
1987-03-00
Pages
1293-5
Language
English
Region
United States
NLM ID
8109087
PMCID
PMC365207
Subset
IM
Grants
NIGMS NIH HHS · GM22135 · United States
External Links
PubMed source DOI: 10.1128/mcb.7.3.1293-1295.1987 PMC Full Text View journal details
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