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中华医学会第十二次全国内分泌学学术会议

作者： Yi Wang Qiongyue Zhang Jianzhi Yang Xiaolong Zhao Min He Xuefei Shou Shiqi Li Yiming Li Yongfei Wang Hongying Ye department of Endocrinology and Metabolism Huashan HospitalFudan University Assistant Reproductive Technology Center First Maternity and Infant Health Hospital Tongji University department of nerosurgery Huashan HospitalFudan University

Context Hypopituitarism is defined as the partial or complete defect of anterior pituitary hormone secretion,may result from pituitary macroadenoma or other sella region tumors,also not rare after pituitary *** with h...

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Mechanism of the Rpn13-induced activation of Uch37

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Protein & Cell 2014年第8期5卷 616-630页

作者： Lianying Jiao Songying Ouyang Neil Shaw Gaojie Song Yingang Feng Fengfeng Niu Weicheng Qiu Hongtao Zhu Li-Wei Hung Xiaobing Zuo V. Eleonora Shtykova Ping Zhu Yu-Hui Dong Ruxiang Xu Zhi-Jie Liu National Laboratory of Biomacromolecules Institute of Biophysics Chinese Academy of Sciences Beijing 100101 China iHuman Institute ShanghaiTech University Shanghai 201210 China Shandong Provincial Key Laboratory ofEnergy-Genetics Qingdao Institute of Bioenergy and Bioprocess TechnologyChinese Academy of Sciences Qingdao 266101 China Physics Division 'Los Alamos National Laboratory Los Alamos NM 87545 USA X-ray Science Division Argonne National Laboratory 9700 South Cass Avenue Argonne IL 60439 USA Institute of Crystallography~ Russian Academy of Sciences 59 Leninsky Pr. 117333 Moscow Russian Federation Center for Multi-disciplinary Research Institute of High Energy Physics Chinese Academy of Sciences Beijing 100049China department of nerosurgery The Military General Hospital of Beijing PLA Beijing 100700 China

Uch37 is a de-ubiquitinating enzyme that is activated by Rpn13 and involved in the proteasomal degradation of proteins. The full-length Uch37 was shown to exhibit low iso-peptidase activity and is thought to be auto-inhibited. Structural comparisons revealed that within a homo- dimer of Uch37, each of the catalytic domains was blocking the other＇s ubiquitin （Ub）-binding site. This blockage likely prevented Ub from entering the active site of Uch37 and might form the basis of auto-inhibition. To understand the mode of auto-inhibition clearly and shed light on the activation mechanism of Uch37 by Rpn13, we investigated the Uch37-Rpn13 complex using a combi- nation of mutagenesis, biochemical, NMR, and small- angle X-ray scattering （SAXS） techniques. Our results also proved that Uch37 oligomerized in solution and had very low activity against the fluorogenic substrate ubi- quitin-7-amino-4-methylcoumarin （Ub-AMC） of de-ubiq- uitinating enzymes. Uch37AHb＇Hc＇KEKE, a truncation removal of the C-terminal extension region （residues 256- 329） converted oligomeric Uch37 into a monomeric form that exhibited iso-peptidase activity comparable to that of a truncation-containing the Uch37 catalytic domain only. We also demonstrated that Rpn13C （Rpn13 residues 270- 407） could disrupt the oligomerization of Uch37 by sequestering Uch37 and forming a Uch37-Rpn13 com- plex. Uch37 was activated in such a complex, exhibiting 12-fold-higher activity than Uch37 alone. Time-resolved SAXS （TR-SAXS） and FRET experiments supported the proposed mode of auto-inhibition and the activation mechanism of Uch37 by Rpn13. Rpn13 activated Uch37 by forming a 1：1 stoichiometric complex in which the active site of Uch37 was accessible to Ub.

关键词： Uch37-Rpn13 complex de-ubiquitination,SAXS analysis oligomerization iso-peptidase

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