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首页> 外文期刊>Biochemistry >DNA-dependent protein kinase phosphorylation sites in Ku 70/80 heterodimer.
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DNA-dependent protein kinase phosphorylation sites in Ku 70/80 heterodimer.

机译：Ku 70/80异二聚体中的DNA依赖性蛋白激酶磷酸化位点。

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摘要

Ku antigen is composed of 70 and 82 kDa subunits (Ku70 and Ku80, respectively) that together bind with high affinity to ends of double-stranded DNA and other DNA structures in vitro. When bound to DNA, the Ku 70/80 heterodimer enhances the kinase activity of the catalytic subunit of the DNA-dependent protein kinase, DNA-PKcs. Ku and DNA-PKcs are required for V(D)J recombination and DNA double-strand break repair in vivo and may also play a role in regulation of transcription. Ku is phosphorylated by DNA-PKcs in vitro, and cells that lack DNA-PKcs are deficient in Ku phosphorylation in vitro, suggesting that Ku may be a physiological target for DNA-PK. Here we have identified the sites of DNA-PK phosphorylation in human Ku protein. We find that Ku70 is phosphorylated at a single serine residue, serine 6, located in the putative transcriptional activation domain, and Ku80 is phosphorylated at serines 577 and 580 and at threonine 715. Interestingly, none of the phosphorylation sites identified in Ku correspond to the serine-glutamine consensus for DNA-PK phosphorylation, consistent with previous reports that DNA-PK can recognize additional phosphorylation motifs.
机译：Ku抗原由70和82 kDa的亚基（分别为Ku70和Ku80）组成，它们在体外与双链DNA和其他DNA结构的末端具有高亲和力。当与DNA结合时，Ku 70/80异二聚体增强了DNA依赖性蛋白激酶DNA-PKcs催化亚基的激酶活性。在体内进行V（D）J重组和DNA双链断裂修复需要Ku和DNA-PKcs，它们也可能在转录调节中起作用。 Ku在体外被DNA-PKcs磷酸化，缺少DNA-PKcs的细胞在体外Ku磷酸化不足，这表明Ku可能是DNA-PK的生理靶标。在这里，我们确定了人类Ku蛋白中DNA-PK磷酸化的位点。我们发现，Ku70在位于假定的转录激活结构域的单个丝氨酸残基丝氨酸6上被磷酸化，而Ku80在丝氨酸577和580以及苏氨酸715上被磷酸化。有趣的是，在Ku中鉴定出的磷酸化位点均不对应于丝氨酸-谷氨酰胺对DNA-PK磷酸化的共识，与以前的报道一致，即DNA-PK可以识别其他磷酸化基序。

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