Ulp1-SUMO crystal structure and genetic analysis reveal conserved interactions and a regulatory element essential for cell growth in yeast
Ulp1-SUMO crystal structure and genetic analysis reveal conserved interactions and a regulatory element essential for cell growth in yeast
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DOI：
10.1016/s1097-2765(00)80326-3
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发表时间：
2000-05-01
期刊：
影响因子：
16
通讯作者：
Lima, CD
中科院分区：
文献类型：
--
作者：
Mossessova, E;Lima, CD
类泛素蛋白SUMO对细胞蛋白质的修饰对于酵母的核过程和细胞周期进程至关重要。Ulp1蛋白酶在SUMO途径中催化两个关键功能：（1）将全长SUMO加工成其成熟形式；（2）将SUMO从靶蛋白上解离下来。对蛋白水解反应的选择性抑制产生了Ulp1的一个C末端片段与其细胞底物Smt3（酵母SUMO同系物）之间的共价硫代半缩醛过渡态复合物。Ulp1 - Smt3的晶体结构以及对保守界面内各元件的功能测试阐明了SUMO识别、加工和解离的决定因素。在该结构指导下进行的遗传分析进一步揭示了蛋白水解结构域N末端的一个调控元件，它是酵母细胞生长所必需的。
Modification of cellular proteins by the ubiquitin-like protein SUMO is essential for nuclear processes and cell cycle progression in yeast. The Ulp1 protease catalyzes two essential functions in the SUMO pathway: (1) processing of full-length SUMO to its mature form and (2) deconjugation of SUMO from targeted proteins. Selective reduction of the proteolytic reaction produced a covalent thiohemiacetal transition state complex between a Ulp1 C-terminal fragment and its cellular substrate Smt3, the yeast SUMO homolog. The Ulp1-Smt3 crystal structure and functional testing of elements within the conserved interface elucidate determinants of SUMO recognition, processing, and deconjugation. Genetic analysis guided by the structure further reveals a regulatory element N-terminal to the proteolytic domain that is required for cell growth in yeast.