Rice, A. P., Kostura, M., Mathews, M. B. (December 1989) Identification of a 90-kDa polypeptide which associates with adenovirus VA RNAI and is phosphorylated by the double-stranded RNA-dependent protein kinase. J Biol Chem, 264 (34). pp. 20632-7. ISSN 0021-9258
Abstract
Interferon treatment of mammalian cells induces a double-stranded (ds) RNA-dependent protein kinase known as DAI. When activated, DAI phosphorylates the alpha-subunit of eukaryotic initiation factor eIF-2, impairing its ability to be recycled and leading to the inhibition of protein synthesis. We have identified a novel DAI substrate in the ribosomal salt wash of rabbit reticulocyte lysates. This substrate is a 90-kDa polypeptide which has been purified to apparent homogeneity. It can be cross-linked by ultraviolet irradiation to adenovirus VA RNAI, a small RNA polymerase III transcript RNA which acts as an inhibitor of DAI. As assayed by a nitrocellulose filter binding assay, the 90-kDa polypeptide is also able to associate with authentic double-stranded RNA, but not single-stranded RNA, made in vitro. Thus, this newly identified substrate of DAI appears to have affinity for dsRNA structures and may be involved in dsRNA-regulated processes in the reticulocyte. Polyclonal and monoclonal antibodies directed against the 90-kDa polypeptide co-precipitate DAI, suggesting that these two proteins may exist as a complex.
Item Type: | Paper |
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Uncontrolled Keywords: | Adenoviruses, Human/*metabolism Animals Antibodies Antigen-Antibody Complex/analysis Electrophoresis, Polyacrylamide Gel Hela Cells/metabolism Humans Molecular Weight Phosphorylation Protein Kinases/*metabolism RNA, Viral/biosynthesis/isolation & purification/*metabolism Rabbits Research Support, U.S. Gov't, P.H.S. Reticulocytes/metabolism Viral Proteins/isolation & purification/*metabolism eIF-2 Kinase |
Subjects: | bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > RNAi organism description > virus > adenovirus bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > polypeptides |
CSHL Authors: | |
Communities: | CSHL labs |
Depositing User: | Gail Sherman |
Date: | 5 December 1989 |
Date Deposited: | 27 Jun 2017 16:03 |
Last Modified: | 27 Jun 2017 16:03 |
Related URLs: | |
URI: | https://repository.cshl.edu/id/eprint/34898 |
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