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PMID: 283387 Published · ppublish English Journal Article

Isolation of two interferon-induced translational inhibitors: a protein kinase and an oligo-isoadenylate synthetase.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 75 ·No. 10 ·1978-10-00 ·Pages 4734-8

Zilberstein A, Kimchi A, Schmidt A, Revel M

Abstract

Large-scale purification of translational inhibitors present in interferon-treated mouse L cells, but not in untreated cells, led to the isolation of two interferon-induced activities. One is a protein kinase system that is activatable by double-stranded RNA and ATP and that phosphorylates a Mr 67,000 protein and the smallest subunit of eukaryotic initiation factor-2. The purified protein kinase is a strong translational inhibitor. The second activity is an enzyme that, with double-stranded RNA, slowly polymerizes ATP into oligoadenylate with a 2'-5' phosphodiester linkage. The oligo-isoadenylate in turn activates a potent inhibitor of mRNA translation.

MeSH Terms
Enzyme Induction Interferons/pharmacology L Cells Nucleotidyltransferases/isolation & purification Peptide Initiation Factors/antagonists & inhibitors Protein Biosynthesis/drug effects Protein Kinases/isolation & purification
Chemicals
Peptide Initiation Factors Interferons Protein Kinases Nucleotidyltransferases
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Zilberstein A
Kimchi A
Schmidt A
Revel M
References (28)
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.75.10.4734
Published
1978-10-00
Pages
4734-8
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC336194
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.75.10.4734 PMC Full Text View journal details
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