A new cAMP independent protein kinase tightly bound to DNA, in rat liver nuclei.
A protein kinase has been characterized among the proteins tightly bound to DNA. It is not extracted with 1 M NaCl and is released by extensive DNase I digestion. This enzyme is able to phosphorylate nucleosomal histones, essentially H2B and H3, and several non-histone proteins associated with DNA, on serine residue(s). It does not phosphorylate protamine, casein, phosvitin and the chromosomal non-histone proteins extracted with 1 M NaCl and is cAMP independent. This protein kinase can be distinguished from the previously described enzymes.
D000818:Animals; D002467:Cell Nucleus / Q000201:enzymology; D000242:Cyclic AMP / Q000378:metabolism*; D004247:DNA / Q000378:metabolism*; D003850:Deoxyribonuclease I; D004706:Endodeoxyribonucleases / Q000378:metabolism; D008099:Liver / Q000201:enzymology*; D008297:Male; D011494:Protein Kinases / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains; D013379:Substrate Specificity
D004247:DNA; D000242:Cyclic AMP; D011494:Protein Kinases; D004706:Endodeoxyribonucleases; D003850:Deoxyribonuclease I