Purification and properties of the double-stranded RNA-activated eukaryotic initiation factor 3 kinase from rabbit reticulocytes.
- 1 November 1980
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 77 (11) , 6526-6530
- https://doi.org/10.1073/pnas.77.11.6526
Abstract
The double-stranded (ds) RNA-activated protein kinase (DAI) that phosphorylates the .alpha. subunit of the eukaryotic initiation factor eIF-2 and inhibits chain initiation was 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. 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 and the .alpha. subunit of eIF-2. After interaction with dsRNA, the enzyme phosphorylates itself and is thereby activated to phosphorylate .alpha. eIF-2 and histone.This publication has 27 references indexed in Scilit:
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