Solution structure of SUMO from Trypanosoma brucei and its interaction with Ubc9
Solution structure of SUMO from Trypanosoma brucei and its interaction with Ubc9
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DOI：
10.1002/prot.22409
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发表时间：
2009-07
期刊：
影响因子：
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通讯作者：
Q. Shang;Chao Xu;Jiahai Zhang;Xuecheng Zhang;X. Tu
中科院分区：
文献类型：
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作者：
Q. Shang;Chao Xu;Jiahai Zhang;Xuecheng Zhang;X. Tu
SUMO(小泛素相关修饰物)的翻译后修饰是调控多种细胞功能的重要机制，如核转运、基因表达、应激反应、细胞周期调控、肿瘤发生和对病毒感染的应答。1-3 SUMO蛋白通过涉及相扑激活酶E1(Aos1/Uba2，又称SAE1/SAE2)、4-6 SUMO结合酶E2(Ubc9)、7，8和E3连接酶的级联酶与靶蛋白连接。布鲁氏锥虫是一种单细胞原生动物，是非洲昏睡病的病原体。布鲁氏锥虫(TB-SUMO)中的相扑序列与人类相扑1和酵母Smt3的序列分别有37%和33%的同源性(支持信息图S1a)。在这里，用核磁共振波谱测定了截短的布鲁氏毛滴虫TB-SUMO(残基7-108)的溶液结构。用核磁共振波谱测定了其与人Ubc9的相互作用表面。这是在原始体中确定的第一个相扑结构。TB-相扑的三维结构与相扑-1和Smt3高度保守。TB-SUMO通过位于TbSUMO b-折叠上的残基与人Ubc9相互作用，这也与SUMO-1和Smt3相似。所有这些结果都表明真核生物中相扑和相扑的进化保守。
Post-translational modification by SUMO (small ubiquitin-related modifier) is an important mechanism that regulates a wide variety of cellular functions, such as nuclear transport, gene expression, stress response, cell cycle control, oncogenesis, and response to virus infection.1–3 SUMO proteins are conjugated to target proteins by an enzymatic cascade involving SUMO activating enzyme E1 (Aos1/Uba2, also named SAE1/SAE2),4–6 SUMO conjugating enzyme E2 (Ubc9),7,8 and E3 ligase. Trypanosoma brucei, the causative agent of African sleeping sickness, is a unicellular protozoan. The sequences of SUMO in Trypanosoma brucei (Tb-SUMO) are 37% and 33% identical with that of human SUMO-1 and yeast Smt3, respectively (Supporting Information Figure S1A). Here, the solution structure of truncated Tb-SUMO (residues 7–108) from T. brucei was determined by NMR spectroscopy. Its interaction surface with human Ubc9 was also determined by chemical shift perturbation using NMR spectroscopy. This is the first structure of SUMO determined in protist. The 3D structure of Tb-SUMO is highly conserved with that of SUMO-1 and Smt3. Tb-SUMO interacts with human Ubc9 through residues located on the b-sheet of TbSUMO, which is also similar to that of SUMO-1 and Smt3. All these results suggest the evolutionary conservation of SUMO and sumoylation in eukaryotes.