In vitro Autophosphorylation and Cyclic Nucleotide-Dependent Dephosphorylation of Sea Urchin Sperm Histone Kinase

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We identified two phosphorylatable proteins (33 kDa and 48 kDa) in crude extractes of spermatozoa from the sea urchin, Hemicentrotus pulcherrimus. While the 33 kDa protein was phosphorylated in 100 mM Mg^<2+>-containing medium with cAMP or cGMP, phosphorylation of the 48 kDa protein occurred irrespective of the Mg^<2+>-concentration if it was more than 10 mM. Physiological concentration if it was more than 10 mM. Physiological concentrations of cAMP or cGMP triggered dephosphorylation of the [^<32>P]-phosphorylated 48 kDa protein in a concentration dependent manner. The dephosphorylation of 48 kDa protein was inhibited with calyculin A or okadaic acid. The 48 kDa protein was associated with a 39 kDa protein to form a larger oligomer with about 400 kDa. The purified 400 kDa protein showed cyclic nucleotide-dependent histone kinase activity. The histone kinase activity shifted from 400 kDa to 39 kDa on a Superose 6 HR in the presence of 5×10^<-6>M cAMP. Phosphorylation of the 48 kDa protein in the purified 400 kDa protein required only Mg[^<32>P]ATP. A photoaffinity cAMP analogue, 8-N_3-[^<32>P]cAMP, was incorporated into the 48 kDa protein. These results suggest that the 48 kDa protein which is a reguratory subunit of the histone kinase is autophosphorylated, and binding of cAMP to the phosphorylated 48 kDa subunit of the kinase results in dissociation of the 48 kDa subunit(s) from the 39 kDa subunit(s) to allow the 48 kDa subunit accessible to a protein phosphatase.
社団法人日本動物学会の論文
1994-04-15

In vitro Autophosphorylation and Cyclic Nucleotide-Dependent Dephosphorylation of Sea Urchin Sperm Histone Kinase

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