Phosphorylation of acid-soluble chromatin proteins from tissues of different species by purified cyclic GMP-dependent protein kinase.
1. Phosphorylation of acid-soluble chromatin proteins from thymus or liver of calf, rabbit, pig, rat, rooster and trout by purified cyclic GMP-dependent protein kinase was studied in vitro using acetic acid-urea slab gel electrophoresis and autoradiography. 2. HMG 14, histone H1 and an unknown band representing probably a proteolytic fragment of histone H1 were phosphorylated in all mammals studied. 3. In avian liver, HMG 14 showed no phosphorylation and histone H1 was replaced by a H1(0)/H5-like heavily phosphorylated protein. 4. The only 32P-acceptor in trout liver apparently belongs to the C/D-family of acid-soluble chromatin proteins. H6-protein was not phosphorylated.
Linnala-Kankkunen
A
A
Department of Biochemistry, University of Kuopio, Finland.
Palvimo
J
J
Mäenpää
P H
PH
D000818:Animals; D002843:Chromatin / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D006657:Histones / Q000378:metabolism; D008099:Liver / Q000378:metabolism; D009687:Nuclear Proteins / Q000378:metabolism*; D010766:Phosphorylation; D011494:Protein Kinases / Q000378:metabolism*; D013045:Species Specificity; D013950:Thymus Gland / Q000378:metabolism
D002843:Chromatin; D006657:Histones; D009687:Nuclear Proteins; D011494:Protein Kinases