Biochemistry international 1988-07-01

Comparison of phosphorylation sites in protamines between protein kinase C and cAMP-dependent protein kinase.

K Nishiyama, K Sakai, Y Tanaka, T Kobayashi, S Nakamura, Y Sakanoue, E Hashimoto, H Yamamura

Index: Biochem. Int. 17(1) , 51-8, (1988)

Full Text: HTML

Abstract

Phosphorylation sites of protamines by protein kinase C and cAMP-dependent protein kinase (protein kinase A) were studied. Using clupeine Y1 as a substrate, protein kinase C phosphorylates both Ser and Thr residues, whereas protein kinase A phosphorylates only Ser residue(s). Protein kinase C phosphorylates all Ser and Thr residues of clupeine Y2 and Z, however protein kinase A phosphorylates mainly Ser9 and slightly Thr5 in clupeine Y2 and Ser6 and Ser10 in clupeine Z. These results suggest that protein kinase C recognizes more sites than those of protein kinase A and may participate in protamine phosphorylation in vivo.

Related Compounds

  • Protamine sulfate...

Related Articles:

DNA and protein footprinting analysis of the modulation of DNA binding by the N-terminal domain of the Saccharomyces cerevisiae TATA binding protein.

2007-09-04

[Biochemistry 46 , 9886-98, (2007)]

Enhancing effect of polyamines on yield of film sarcoma.

1984-04-01

[Eur. J. Cancer Clin. Oncol. 20(4) , 503-6, (1984)]

The binding mode of a mammalian (boar) protamine to DNA.

1988-01-01

[Biochem. Int. 16(1) , 163-73, (1988)]

Nuclear magnetic resonance of protamines. A 1H-NMR study of the interaction of clupeine fractions with mononucleotides.

1986-05-05

[Biochim. Biophys. Acta 866(4) , 216-21, (1986)]

Nature of protamine-DNA complexes. A special type of ligand binding co-operativity.

1991-11-20

[J. Mol. Biol. 222(2) , 423-33, (1991)]

More Articles...