Phosphorylation of high mobility group protein HMG 14 by a cyclic GMP-dependent protein kinase from avian liver nucleoli

1981 ◽  
Vol 654 (2) ◽  
pp. 287-291 ◽  
Author(s):  
Annikka Linnala-Kankkunen ◽  
Pekka H. Mäenpää
Keyword(s):  
Protein Kinase ◽  
Cyclic Gmp ◽  
High Mobility ◽  
High Mobility Group ◽  
High Mobility Group Protein ◽  
Dependent Protein Kinase ◽  
Dependent Protein ◽  
Group Protein

scholarly journals Phosphorylation of high mobility group 1 protein by phospholipid-sensitive Ca2+-dependent protein kinase from pig testis

1985 ◽  
Vol 227 (1) ◽  
pp. 271-276 ◽  
Author(s):  
K Kimura ◽  
N Katoh ◽  
K Sakurada ◽  
S Kubo
Keyword(s):  
Protein Kinase ◽  
High Mobility ◽  
Particulate Fraction ◽  
High Mobility Group ◽  
Hmg Proteins ◽  
Dependent Protein Kinase ◽  
Histone Proteins ◽  
Km Value ◽  
Dependent Protein ◽  
Group 1

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.

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