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首页> 外文期刊>Biochemistry >Phosphorylation of human p53 on Thr-55.
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Phosphorylation of human p53 on Thr-55.

机译：人p53在The-55上的磷酸化。

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摘要

The pleiotropic function of p53 is believed to be greatly influenced by phosphorylation, and several sites on p53 are known to be targets for distinct protein kinases. In this study, we observed that affinity-purified p53 from overexpressing cells was phosphorylated by a co-purified protein kinase in vitro. To identify phosphorylation site(s), the resulting phosphorylated p53 protein was subjected to primary and secondary proteolytic cleavage, and phosphopeptides were fractionated by a two-dimensional peptide gel system. Phosphoamino acid analysis and manual Edman degradation of the isolated phosphopeptides enabled us to unequivocally identify Thr-55 as the major phosphorylation site on p53. Furthermore, comparative phosphopeptide mapping data suggest that DNA-PK is not the kinase responsible for this phosphorylation. Significantly, using a phospho-specific antibody for Thr-55, we have shown that Thr-55 is indeed phosphorylated in vivo. These data define Thr-55 as a novel phosphorylation site and for the first time show threonine phosphorylation of human p53.
机译：据信p53的多效性功能受磷酸化的影响很大，并且已知p53上的几个位点是不同蛋白激酶的靶标。在这项研究中，我们观察到过表达细胞中亲和纯化的p53在体外被共纯化的蛋白激酶磷酸化。为了鉴定磷酸化位点，将所得的磷酸化的p53蛋白进行一级和二级蛋白水解切割，并通过二维肽凝胶系统分级分离磷酸肽。磷酸氨基酸分析和分离的磷酸肽的手动Edman降解使我们能够清楚地确定Thr-55是p53上的主要磷酸化位点。此外，比较的磷酸肽作图数据表明，DNA-PK不是负责该磷酸化的激酶。重要的是，使用针对Thr-55的磷酸特异性抗体，我们已经显示Thr-55在体内确实被磷酸化了。这些数据将Thr-55定义为一个新的磷酸化位点，并首次显示人p53的苏氨酸磷酸化。

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