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PMID: 6935666 Published · ppublish English Journal Article

Purification and properties of the double-stranded RNA-activated eukaryotic initiation factor 3 kinase from rabbit reticulocytes.

Grosfeld H, Ochoa S

Abstract

The double-stranded RNA (dsRNA)-activated protein kinase (DAI) that phosphorylates the alpha subunit of the eukaryotic initiation factor eIF-2 and inhibits chain initiation has been isolated from rabbit reticulocyte lysates. The nonactivated enzyme or the enzyme partially activated by incubation with low levels of dsRNA (pro-DAI) could be purified only to a slight extent. However, the enzyme that was fully activated by incubation with both dsRNA and ATP was purified to near homogeneity. Active DAI is a phosphoprotein with an apparent subunit mass of 68,000 daltons. It can phosphorylate histone as well as the alpha subunit of eIF-2. Our results suggest that, after interaction with dsRNA, the enzyme phosphorylates itself and is thereby activated to phosphorylate alpha eIF-2 and histone.

MeSH Terms
Animals Enzyme Activation Histones/metabolism Peptide Initiation Factors/metabolism Phosphoproteins/isolation & purification,metabolism Phosphorylation Protein Kinases/isolation & purification,metabolism RNA, Double-Stranded/metabolism Rabbits Reticulocytes/enzymology
Chemicals
Histones Peptide Initiation Factors Phosphoproteins RNA, Double-Stranded Protein Kinases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Grosfeld H
Ochoa S
References (27)
27 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
Published
1980-11-00
Pages
6526-30
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC350318
Subset
IM
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