| Literature DB >> 3202865 |
T H Carter1, C R Kopman, C B James.
Abstract
Incorporation of 32P from gamma-labeled ATP into a number of polypeptides in HeLa whole cell and nuclear extracts was dependent on added double-stranded DNA or poly(dI-dC), but not denatured or supercoiled DNA. DNA-dependent phosphorylation of a high Mr endogenous substrate could be reconstituted from the precipitate formed after incubation of whole cell extracts with DNA. Fractionation of extracts by phosphocellulose or DEAE-Sephacel chromatography yielded preparations that phosphorylated casein as well as endogenous polypeptides in a DNA-dependent manner. These results are consistent with the existence of a novel protein kinase in HeLa cells that is highly dependent upon the presence of double-stranded DNA for efficient phosphorylation of a variety of substrates.Entities:
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Year: 1988 PMID： 3202865 DOI： 10.1016/s0006-291x(88)80282-1
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN： 0006-291X Impact factor: 3.575