Unrestrictive identification of non-phosphorylation PTMs in yeast kinases by MS and PTMap.
Unrestrictive identification of non-phosphorylation PTMs in yeast kinases by MS and PTMap.
复制标题
DOI：
10.1002/pmic.200900510
复制
发表时间：
2010-03
期刊：
影响因子：
3.4
通讯作者：
Zhao, Yingming
中科院分区：
文献类型：
--
作者：
Zhang, Kai;Chen, Yue;Zhang, Zhihong;Tao, Shengce;Zhu, Heng;Zhao, Yingming
已知一些蛋白质PTM，如磷酸化和泛素化，在调节蛋白激酶活性中至关重要。然而，其他PTM的作用尚未在激酶中得到广泛研究。开发所有类型的PTM的综合描述和发现低丰度的新型体内PTM代表了主要的分析挑战。为了实现这一目标，我们已经开发了一种策略，用于系统和准确地鉴定酵母蛋白激酶中的全谱PTM。我们的策略包括GST融合激酶蛋白的分离，MS分析，和PTMap算法的非限制性PTM鉴定。在30个纯化的酵母激酶中，我们鉴定了27种不同类型的PTM，和53个PTM位点，其中13个新的质量位移，以前没有报道，可能代表新的PTM。这些结果代表了我们目前对激酶中PTM的理解的显著扩展，并表明激酶功能的高度复杂调节。
A few protein PTMs, such as phosphorylation and ubiquitination, are known to be critical in regulation of protein kinase activities. However, the roles of other PTMs have not been extensively studied in kinases. Development of a comprehensive description of all types of PTMs and discovering novel in vivo PTMs in low abundance represent major analytical challenges. Toward this goal, we have developed a strategy for systematic and accurate identification of the full-spectrum of PTMs in yeast protein kinases. Our strategy involves isolation of GST-fused kinase proteins, MS analysis, and unrestrictive PTM identification by PTMap algorithm. Among the 30 purified yeast kinases, we identified 27 different types of PTMs, and 53 PTM sites, among which are 13 novel mass shifts that have not been previously reported, likely representing novel PTMs. These results represent a significant expansion of our current understanding of PTMs in kinases and suggest highly complex regulation of kinase function.
登录
查看更多内容
影响因子：
64.8
作者：
Ptacek, J;Devgan, G;Snyder, M
通讯作者：
Snyder, M
影响因子：
7.5
作者：
Martin, Cyrus;Zhang, Yi
通讯作者：
Zhang, Yi
影响因子：
21.3
作者：
Cohen, P
通讯作者：
Cohen, P
影响因子：
4.4
作者：
Chen, Y;Kwon, SW;Zhao, YM
通讯作者：
Zhao, YM
影响因子：
11.2
作者：
Contessa, Joseph N.;Bhojani, Mahaveer S.;Lawrence, Theodore S.
通讯作者：
Lawrence, Theodore S.