Molecular evolution of type 1 serine/threonine protein phosphatases
Molecular evolution of type 1 serine/threonine protein phosphatases
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DOI：
10.1006/mpev.1998.0560
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发表时间：
1999-06-01
影响因子：
4.1
通讯作者：
Walker, JC
中科院分区：
文献类型：
--
作者：
Lin, Q;Buckler, ES;Walker, JC
1型丝氨酸/苏氨酸蛋白磷酸酶（PP 1）在许多细胞过程中起着关键作用。为了了解不同界的PP 1之间的进化关系，并提供一个有效的基础，以评估这些磷酸酶的结构-功能关系，44 PP 1序列进行了比对，揭示了PP 1同源物之间的高度序列相似性。在所研究的所有序列中，约三分之一的氨基酸是保守的。这些保守氨基酸中的大多数位于270个氨基酸的核心区域内。基于哺乳动物PP 1的三维结构研究，它们包括对PP 1的活性和调节至关重要的大多数位点。使用滑动窗口方法的位置变异分析揭示了270个氨基酸的核心区域中的两个可变块。主要可变区对应于由三个α-螺旋（α G、α H和α I）和三个β-折叠（β 7、β 8和β 9）组成的子域。系统发育分析表明，植物和动物PP 1形成不同的单系群。植物PP 1家族包含几个可能比单子叶-双子叶分歧更古老的亚群。在动物PP 1家族中，不同的脊椎动物同种型似乎形成不同的亚组。相对替代率研究表明，植物PP 1 s比动物PP 1 s更多样化，平均替代率是动物PP 1 s的1.5倍。PP 1 s在建立多细胞性的可能参与进行了讨论。(C)北京：科学出版社.
Type 1 serine/threonine protein phosphatases (PP1s) play key roles in many cellular processes. To understand the evolutionary relationships among PP1s from various kingdoms and to provide a valid basis to evaluate the structure-function relationships of these phosphatases, 44 PP1 sequences were aligned, revealing a high sequence similarity among PP1 homologs. About one-third of the total amino acids are conserved in all the sequences studied. Most of these conserved amino acids are located within a 270-amino-acid core region. They include most sites critical to the activity and regulation of PP1s based on three-dimensional structural studies of mammalian PP1s. Positional variation analysis using a sliding window approach revealed two variable blocks in the 270-amino-acid core region. The major variable block corresponds to a subdomain composed of three alpha-helices (alpha G, alpha H, and alpha I) and three beta-sheets (beta 7, beta 8, and beta 9). Phylogenetic analyses suggested that plant and animal PP1s form distinct monophyletic groups. The plant PP1 family contains several subgroups that may be older than the monocot-dicot divergence. In the animal PP1 family, different vertebrate isoforms appear to form distinct subgroups. Relative substitution rate studies indicated that plant PP1s are more diverse than animal PP1s, with an average substitution rate 1.5 times as large as that of animal PP1s. The possible involvement of PP1s in the establishment of multicellularity is discussed. (C) 1999 Academic Press.