嗜热嗜甲烷菌Methanosarcina thermophila TM-1毒素敏感蛋白磷酸酶的基因克隆、表达及特性分析
Gene cloning and expression and characterization of a toxin-sensitive protein phosphatase from the methanogenic archaeon Methanosarcina thermophila TM-1.
作者信息
Solow B, Young J C, Kennelly P J
机构信息
Department of Biochemistry, Virginia Polytechnic Institute and State University, Blacksburg 24061-0308, USA.
出版信息
J Bacteriol. 1997 Aug;179(16):5072-5. doi: 10.1128/jb.179.16.5072-5075.1997.
Abstract
With oligonucleotides modelled after conserved regions within the protein-serine/threonine phosphatases (PPs) of the PP1/2A/2B superfamily, the gene for the archaeal protein phosphatase PP1-arch2 was identified, cloned, and sequenced from the methanogenic archaeon Methanosarcina thermophila TM-1. The DNA-derived amino acid sequence of PP1-arch2 exhibited a high degree of sequence identity, 27 to 31%, with members of the PP1/2A/2B superfamily such as PP1-arch1 from Sulfolobus solfataricus, PP1alpha from rats, PP2A from Saccharomyces cerevisiae, and PP2B from humans. The activity of the recombinant PP1-arch2 was sensitive to several naturally occurring microbial toxins known to potently inhibit eucaryal PP1 and PP2A, including microcystin-LR, okadaic acid, tautomycin, and calyculin A.
摘要
利用基于PP1/2A/2B超家族蛋白质丝氨酸/苏氨酸磷酸酶（PP）保守区域构建的寡核苷酸，从嗜热产甲烷古菌嗜热甲烷八叠球菌TM-1中鉴定、克隆并测序了古菌蛋白质磷酸酶PP1-arch2的基因。PP1-arch2的DNA推导氨基酸序列与PP1/2A/2B超家族成员，如来自嗜热栖热菌的PP1-arch1、来自大鼠的PP1α、来自酿酒酵母的PP2A和来自人类的PP2B，表现出高度的序列同一性，为27%至31%。重组PP1-arch2的活性对几种已知能有效抑制真核生物PP1和PP2A的天然微生物毒素敏感，包括微囊藻毒素-LR、冈田酸、互隔交链孢酚单甲醚和花萼海绵诱癌素A。
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