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首页> 外文期刊>Biochimica et Biophysica Acta. Protein Structure and Molecular Enzymology >Phosphorylation of Mycobacterium leprae heat-shock 70 protein at threonine 175 alters its substrate binding characteristics
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Phosphorylation of Mycobacterium leprae heat-shock 70 protein at threonine 175 alters its substrate binding characteristics

机译：苏氨酸175时麻风分枝杆菌热休克蛋白70的磷酸化改变了其底物结合特性

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摘要

We have examined the functional properties including autophosphorylation of the Mycobacterium leprae Hsp70 homologue. Recombinant M. leprae Hsp70 had pH optima for its adenosine triphosphatase and autophosphorylating activities which were near pH 8 and 6, respectively. Both these activities were inhibited by reduced and alkylated bovine pancreatic trypsin inhibitor, but not other tested substrates. Autophosphorylation was augmented by up to 25 mM Ca~(2+). Using site-directed mutagenesis to construct two Thr → Ala mutants at positions 175 and 193, and phosphoamino acid analysis, it was shown that Thr~(175) was the dominant threonine residue autophosphorylated in M. leprae Hsp70. Phosphorylation led to an increased affinity for a model polypeptide substrate, reduced and alkylated bovine albumin. These properties are compared with those of the DnaK protein of Escherichia coli.
机译：我们已经检查了功能特性，包括麻风分枝杆菌Hsp70同源物的自磷酸化。重组麻风杆菌Hsp70的腺苷三磷酸酶和自磷酸化活性的最适pH分别接近pH 8和6。这两种活性均被还原的和烷基化的牛胰胰蛋白酶抑制剂抑制，但未受其他受试底物抑制。自磷酸化增加了高达25 mM Ca〜（2+）。利用定点诱变在175和193位构建两个Thr→Ala突变体，并进行磷酸氨基酸分析，结果表明Thr〜（175）是麻疯树Hsp70中自磷酸化的主要苏氨酸残基。磷酸化导致对模型多肽底物的亲和力增加，牛白蛋白减少和烷基化。将这些性质与大肠杆菌的DnaK蛋白的性质进行比较。

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