Phosphorylation of high mobility group 1 protein by phospholipid-sensitive Ca2+-dependent protein kinase from pig testis.
Phospholipid-sensitive Ca2+-dependent protein kinase was partially purified from total particulate fraction of pig testis. The enzyme phosphorylated high mobility group 1 protein (HMG 1), one of the major chromatin-associated non-histone proteins. Other HMG proteins (HMG 2, 14 and 17) were not phosphorylated by the enzyme. Exhaustive phosphorylation of HMG 1 revealed that 1 mol of phosphate was incorporated/mol of HMG 1. The apparent Km value for HMG 1 was 3.66 microM. 1,3-Diolein stimulated the phosphorylation at 10 microM-Ca2+ in the presence of phosphatidylserine. The phosphorylation of HMG 1 was inhibited by adriamycin, an inhibitor of spermatogenesis.
Kimura
K
K
Katoh
N
N
Sakurada
K
K
Kubo
S
S
D000818:Animals; D002118:Calcium / Q000494:pharmacology; D004075:Diglycerides / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D006609:High Mobility Group Proteins / Q000378:metabolism*; D007700:Kinetics; D008297:Male; D010766:Phosphorylation; D011493:Protein Kinase C; D011494:Protein Kinases / Q000378:metabolism*; D013552:Swine; D013737:Testis / Q000201:enzymology*
D004075:Diglycerides; D006609:High Mobility Group Proteins; D011494:Protein Kinases; D011493:Protein Kinase C; D002118:Calcium; C013965:diolein