Autophosphorylation of the protein kinase dependent on double-stranded RNA - PubMed (original) (raw)
. 1987 Nov 15;262(32):15538-44.
Affiliations
- PMID: 3479429
Free article
Autophosphorylation of the protein kinase dependent on double-stranded RNA
J Galabru et al. J Biol Chem. 1987.
Free article
Abstract
The double-stranded RNA (dsRNA)-dependent protein kinase (p68 kinase) from interferon-treated human cell is a Mr 68,000 protein induced by interferon. By the use of a specific monoclonal antibody, we have been able to study the two distinct protein kinase activities characteristic of purified p68 kinase. The first activity is functional for endogenous phosphorylation of the enzyme (p68 kinase), whereas the second one is responsible for the phosphorylation of exogenous substrates such as eukaryotic initiation factor 2 and histone. When activated by dsRNA in the presence of Mn2+ and ATP, p68 kinase is autophosphorylated and is then capable of catalyzing phosphorylation of histone in the absence of dsRNA. Whereas binding of 8-azido-[alpha-32P] ATP (8-N3ATP) to p68 kinase is dependent on both dsRNA and Mn2+, phosphorylated p68 kinase binds 8-N3ATP independent of dsRNA. This is consistent with a dsRNA requirement for the autophosphorylation of p68 kinase, but not for the phosphorylation of exogenous substrates. p68 kinase is mainly associated with the ribosomal pellet. It could be recovered efficiently by a buffer containing both high salt and a nonionic detergent. Synthesis of p68 kinase is induced several-fold by interferon in different types of human cells. Partial proteolysis of [35S]methionine and an 8-N3ATP-labeled p68 kinase preparation by Staphylococcus aureus V8 protease indicated the presence of a major Mr 48,000 polypeptide (p48) with a specific ATP-binding site. p48 probably contains the catalytic unit of p68 kinase and is analogous to a similar protein which we have previously described as a distinct protein present in a complexed form with p68 kinase. We now believe that the presence of p48 in previously purified kinase preparations was due to partial degradation of p68 kinase.
Similar articles
- Monoclonal antibodies to an interferon-induced Mr 68,000 protein and their use for the detection of double-stranded RNA-dependent protein kinase in human cells.
Laurent AG, Krust B, Galabru J, Svab J, Hovanessian AG. Laurent AG, et al. Proc Natl Acad Sci U S A. 1985 Jul;82(13):4341-5. doi: 10.1073/pnas.82.13.4341. Proc Natl Acad Sci U S A. 1985. PMID: 3859866 Free PMC article. - Two interferon-induced proteins are involved in the protein kinase complex dependent on double-stranded RNA.
Galabru J, Hovanessian AG. Galabru J, et al. Cell. 1985 Dec;43(3 Pt 2):685-94. doi: 10.1016/0092-8674(85)90241-7. Cell. 1985. PMID: 2416468 - The double-stranded RNA-dependent protein kinase is also activated by heparin.
Hovanessian AG, Galabru J. Hovanessian AG, et al. Eur J Biochem. 1987 Sep 15;167(3):467-73. doi: 10.1111/j.1432-1033.1987.tb13360.x. Eur J Biochem. 1987. PMID: 3653103 - Functional expression and RNA binding analysis of the interferon-induced, double-stranded RNA-activated, 68,000-Mr protein kinase in a cell-free system.
Katze MG, Wambach M, Wong ML, Garfinkel M, Meurs E, Chong K, Williams BR, Hovanessian AG, Barber GN. Katze MG, et al. Mol Cell Biol. 1991 Nov;11(11):5497-505. doi: 10.1128/mcb.11.11.5497-5505.1991. Mol Cell Biol. 1991. PMID: 1717830 Free PMC article. - Interferon-induced and double-stranded RNA-activated enzymes: a specific protein kinase and 2',5'-oligoadenylate synthetases.
Hovanessian AG. Hovanessian AG. J Interferon Res. 1991 Aug;11(4):199-205. doi: 10.1089/jir.1991.11.199. J Interferon Res. 1991. PMID: 1717615 Review.
Cited by
- Interactions between double-stranded RNA regulators and the protein kinase DAI.
Manche L, Green SR, Schmedt C, Mathews MB. Manche L, et al. Mol Cell Biol. 1992 Nov;12(11):5238-48. doi: 10.1128/mcb.12.11.5238-5248.1992. Mol Cell Biol. 1992. PMID: 1357546 Free PMC article. - Mapping of the auto-inhibitory interactions of protein kinase R by nuclear magnetic resonance.
Gelev V, Aktas H, Marintchev A, Ito T, Frueh D, Hemond M, Rovnyak D, Debus M, Hyberts S, Usheva A, Halperin J, Wagner G. Gelev V, et al. J Mol Biol. 2006 Dec 1;364(3):352-63. doi: 10.1016/j.jmb.2006.08.077. Epub 2006 Sep 1. J Mol Biol. 2006. PMID: 17011579 Free PMC article. - Molecular cloning and characterization of an interferon induced human cDNA with sequence homology to a mammalian peptide chain release factor.
Buwitt U, Flohr T, Böttger EC. Buwitt U, et al. EMBO J. 1992 Feb;11(2):489-96. doi: 10.1002/j.1460-2075.1992.tb05079.x. EMBO J. 1992. PMID: 1537332 Free PMC article. - Structural requirements for double-stranded RNA binding, dimerization, and activation of the human eIF-2 alpha kinase DAI in Saccharomyces cerevisiae.
Romano PR, Green SR, Barber GN, Mathews MB, Hinnebusch AG. Romano PR, et al. Mol Cell Biol. 1995 Jan;15(1):365-78. doi: 10.1128/MCB.15.1.365. Mol Cell Biol. 1995. PMID: 7799945 Free PMC article. - The alpha subunit of eucaryotic initiation factor 2 is phosphorylated in mengovirus-infected mouse L cells.
DeStefano J, Olmsted E, Panniers R, Lucas-Lenard J. DeStefano J, et al. J Virol. 1990 Sep;64(9):4445-53. doi: 10.1128/JVI.64.9.4445-4453.1990. J Virol. 1990. PMID: 2166823 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources