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首页> 外文期刊>The Journal of Antibiotics: An International Journal >Self-activation of Serine/Threonine Kinase AfsK on Autophosphorylation at Threonine-168
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Self-activation of Serine/Threonine Kinase AfsK on Autophosphorylation at Threonine-168

机译：丝氨酸/苏氨酸激酶AfsK在苏氨酸168上自磷酸化的自激活

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摘要

A Hanks-type protein kinase AfsK autophosphorylates on threonine residue(s)and phosphorylates AfsR,a global regulator for secondary metabolism in Streptomyces coelicolor A3(2).Mass spectrometry of a tryptic digest of the autophosphorylated form of AfsKAC corresponding to the kinase catalytic domain(Met-1 to Arg-311)of AfsK,together with subsequent site-directed mutagenesis of the candidate amino acids,identified threonine-168 as a single autophosphorylation site.Threonine-168 is located in the activation loop that is known for some Ser/Thr kinases to modulate kinase activity on phosphorylation of one or more threonine residues within the loop.Consistent with this,mutant T168D,in which Thr-168 was replaced by Asp,became a constitutively active kinase;it phosphorylated AfsR to the same eixtent as AfsKAC produced in and purified from Escherichia coli cells during which a considerable population of it had been already phosphorylated intermolecularly.All these findings show that autophosphorylation or intermolecular phosphorylation of threonine-168 in AfsK accounts for the self-activation of its kinase activity.
机译：Hanks型蛋白激酶AfsK在苏氨酸残基上自磷酸化并磷酸化AfsR，一种在链霉菌A3（2）中进行次级代谢的全局调节剂.AfsKAC自磷酸化形式的胰蛋白酶消化物的质谱图（对应于激酶催化域） （Met-1至Arg-311）的AfsK，以及随后对候选氨基酸的定点诱变，将苏氨酸168确定为单个自磷酸化位点。苏氨酸168位于激活环中，该环对于某些Ser已知/ Thr激酶调节环中一个或多个苏氨酸残基磷酸化时的激酶活性。与此相一致的是，突变型T168D（其组成成分为活性激酶，其中Thr-168被Asp取代）;它使AfsR磷酸化为与AfsKAC在大肠杆菌细胞中产生和纯化，在此期间，相当数量的细胞已经被分子间磷酸化了。所有这些发现表明自磷酸化AfsK中苏氨酸168的酰化或分子间磷酸化是其激酶活性的自我激活。

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