Autophosphorylation and Cross-Phosphorylation of Protein Kinases from the Crenarchaeon Sulfolobus islandicus.
Autophosphorylation and Cross-Phosphorylation of Protein Kinases from the Crenarchaeon Sulfolobus islandicus.
复制标题
来自岛状硫化叶菌的蛋白激酶的自磷酸化和交叉磷酸化
DOI：
10.3389/fmicb.2017.02173
复制
发表时间：
2017
影响因子：
5.2
通讯作者：
Shen Y
中科院分区：
文献类型：
--
作者：
Huang Q;Zhong Q;Mayaka JBA;Ni J;Shen Y
蛋白质磷酸化是最重要的翻译后修饰之一，几乎调节着所有的细胞过程。虽然蛋白质磷酸化信号转导在真核生物和细菌中得到了广泛的研究，但对古细菌中这一过程的认识非常滞后，特别是对于真核生物样蛋白激酶（ePKs）的Ser/Thr/Tyr磷酸化。迄今为止，关于古细菌ePKs的研究报道较少，且大多集中在体外磷酸化活性方面，其生理功能和相互作用网络尚不清楚。在本研究中，我们系统地研究了冰岛硫化叶菌REY 15 A的ePKs的自磷酸化和交叉磷酸化活性，使用在大肠杆菌或S.冰岛人。体外激酶活性测定结果表明，在11个推测的ePKs中，有7个具有自磷酸化活性。蛋白质Ser/Thr磷酸酶SiRe_1009能够使各种自磷酸化的ePK去磷酸化，证实这些蛋白质是Ser/Thr激酶。SiRe_2030和SiRe_2056是典型的真核生物PKs的同源物，它们参与响应各种细胞应激的肽合成，对自身和其他ePKs表现出高效的磷酸化活性。体内实验表明，SiRe_1531或SiRe_2056均能抑制S. islandicus细胞最后，提出了蛋白激酶的磷酸化网络，并讨论了它们可能的生理作用。
Protein phosphorylation, one of the most important post-translational modifications, regulates almost every cellular process. Although signal transduction by protein phosphorylation is extensively studied in Eukaryotes and Bacteria, the knowledge of this process in archaea is greatly lagging behind, especially for Ser/Thr/Tyr phosphorylation by eukaryotic-like protein kinases (ePKs). So far, only a few studies on archaeal ePKs have been reported, most of which focused on the phosphorylation activities in vitro, but their physiological functions and interacting network are still largely unknown. In this study, we systematically investigated the autophosphorylation and cross-phosphorylation activities of ePKs from Sulfolobus islandicus REY15A using proteins expressed in Escherichia coli or S. islandicus. In vitro kinase assay showed that 7 out of the 11 putative ePKs have autophosphorylation activity. A protein Ser/Thr phosphatase, SiRe_1009, was able to dephosphorylate various autophosphorylated ePKs, confirming that these proteins are Ser/Thr kinases. Two ePKs, SiRe_2030 and SiRe_2056, homologs of typical eukaryotic PKs involved in peptide synthesis in response to various cellular stresses, exhibit highly efficient phosphorylation activities on both themselves and other ePKs. Overexpression of the protein kinases in vivo revealed that elevated level of either SiRe_1531 or SiRe_2056 inhibited the cell growth of S. islandicus cells. Finally, a phosphorylation network of the protein kinases was proposed and their putative physiological roles were discussed.
登录
查看更多内容
影响因子：
64.5
作者：
Hopkins BB;Paull TT
通讯作者：
Paull TT
影响因子：
3.2
作者：
Frols, Sabrina;Gordon, Paul M. K.;Schleper, Christa
通讯作者：
Schleper, Christa
影响因子：
4.8
作者：
Baer, Christina E.;Iavarone, Anthony T.;Sassetti, Christopher M.
通讯作者：
Sassetti, Christopher M.
影响因子：
11.4
作者：
Hecker, Arnaud;Lopreiato, Raffaele;van Tilbeurgh, Herman
通讯作者：
van Tilbeurgh, Herman
影响因子：
5.4
作者：
Deng, Ling;He, Fei;Peng, Xu
通讯作者：
Peng, Xu