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首页> 外文期刊>Biochemistry >Involvement of Protein Kinase A in the Phosphorylatio of Spermatidal Protein TP2 and Its Effect on DNA Condensation
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Involvement of Protein Kinase A in the Phosphorylatio of Spermatidal Protein TP2 and Its Effect on DNA Condensation

机译：蛋白激酶A在精子蛋白TP2的磷酸化中的参与及其对DNA缩合的影响

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摘要

Rat spermatidal protein TP2 is rich in serine residues and has several potential sites for phosphorylation by different protein kinases. Recombinant TP2 is phosphorylated upon incubation in vitro with salt extract of testicular sonication resistant nucliei (SRN) (representing elongating and elongated spermatids). The major phosphorylation sites were localized to the C-terminal, V8 protease-derived, fragment (residues 87-114). Phosphorylation experiments with the wild type and different site-specific mutants of TP2 revealed that serine 109 and threonine 101 are the phosphorylation sites. Phosphorylation of the C-terminalfragment of TP2 was also demonstrated in vivo. Phosphorylation was not stimulated by either protein kinase C activators or cGMP but was inhibited by protein kinase A inhibitor (PKI) peptide, showing the involvement of protein kinase A in the phosphorylation of TP2. Phosphorylation of TP2 greatly reduced its DNA condensation property. TP2 when complexed with DNA was not a good substrate for phosphorylation by PKA. Dephosphorylation of the DNA-TP2 complex by calf intestinal alkaline phosphatase restored the DNA condensation property to a level equivalent to that observed with TP2. The physiological significance of the phosphorylation-dephosphorylation cycle is discussed with reference to the two-domain model of TP2.
机译：大鼠精子蛋白TP2富含丝氨酸残留物，并通过不同的蛋白激酶具有若干潜在位点。重组TP2在体外孵育时磷酸化，耐药超声抗性核心（SRN）（代表伸长细长的精子）。将主要磷酸化位点定位于C末端，V8蛋白酶衍生的片段（残留物87-114）。 TP2的野生型和不同位点特异性突变体的磷酸化实验显示丝氨酸109和苏氨酸101是磷酸化位点。还在体内进行了TP2的C-末端浆化的磷酸化。蛋白激酶C活化剂或CGMP未刺激磷酸化，但是通过蛋白激酶抑制抑制剂（PKI）肽，显示蛋白激酶A在TP2的磷酸化中的累积。 TP2的磷酸化大大降低了其DNA凝结性能。与DNA复合时的TP2不是PKA磷酸化的良好基材。通过小牛肠碱性磷酸酶去磷酸化DNA-TP2复合物恢复DNA缩合性能与用TP2观察到的水平。参考TP2的两域模型讨论了磷酸化 - 去磷酸化周期的生理意义。

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