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. 1980 Nov;77(11):6526–6530. doi: 10.1073/pnas.77.11.6526

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

H Grosfeld, S Ochoa
PMCID: PMC350318  PMID: 6935666

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.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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