Zeke T, Gergely P, Dombrádi V
Department of Medical Chemistry, University Medical School of Debrecen, Hungary.
Comp Biochem Physiol B Biochem Mol Biol. 1998 Feb;119(2):317-24. doi: 10.1016/s0305-0491(97)00341-6.
The catalytic activities of protein phosphatase 1, 2A, 2B, and 2C were detected in crude extracts of Caenorhabditis elegans with different phosphoprotein substrates and specific inhibitors or activators. The enzymological properties of protein phosphatase 2B as well as those of the catalytic subunits of protein phosphatase 1 and protein phosphatase 2A were determined after partial purification. Gene fragments encoding the catalytic subunits of the protein phosphatase 1-2A-2B superfamily were amplified by polymerase chain reaction and were identified by DNA sequencing. Besides the homologs of protein phosphatase 1, 2B, and X, five protein phosphatase 1-type sequences and four novel protein phosphatase sequences were found. Our data, together with the results of the C. elegans genome project, suggest that this nematode contains an extensive family of Ser/Thr specific protein phosphatases including several up to now biochemically uncharacterized members.
利用不同的磷蛋白底物以及特异性抑制剂或激活剂，在秀丽隐杆线虫的粗提物中检测了蛋白磷酸酶1、2A、2B和2C的催化活性。在部分纯化后，测定了蛋白磷酸酶2B以及蛋白磷酸酶1和蛋白磷酸酶2A催化亚基的酶学性质。通过聚合酶链反应扩增了编码蛋白磷酸酶1 - 2A - 2B超家族催化亚基的基因片段，并通过DNA测序进行了鉴定。除了蛋白磷酸酶1、2B和X的同源物外，还发现了5个蛋白磷酸酶1型序列和4个新的蛋白磷酸酶序列。我们的数据以及秀丽隐杆线虫基因组计划的结果表明，这种线虫含有一个广泛的丝氨酸/苏氨酸特异性蛋白磷酸酶家族，其中包括几个迄今为止在生物化学上尚未表征的成员。
