Mechanism of the Rpn13-induced activation of Uch37

Jiao, Lianying; Ouyang, Songying; Shaw, Neil; Song, Gaojie; Feng, Yingang; Niu, Fengfeng; Qiu, Weicheng; Zhu, Hongtao; Hung, Li-Wei; Zuo, Xiaobing; Eleonora Shtykova, V.; Zhu, Ping; Dong, Yu-Hui; Xu, Ruxiang; Liu, Zhi-Jie

doi:10.1007/s13238-014-0046-z

Mechanism of the Rpn13-induced activation of Uch37

Journal Article · Tue Apr 22 00:00:00 EDT 2014 · Protein & Cell

DOI:https://doi.org/10.1007/s13238-014-0046-z· OSTI ID:1815417

Jiao, Lianying ^[1]; Ouyang, Songying ^[2]; Shaw, Neil ^[2]; Song, Gaojie ^[3]; Feng, Yingang ^[4]; Niu, Fengfeng ^[2]; Qiu, Weicheng ^[2]; Zhu, Hongtao ^[2]; Hung, Li-Wei ^[5]; Zuo, Xiaobing ^[6]; Eleonora Shtykova, V. ^[7]; Zhu, Ping ^[2]; Dong, Yu-Hui ^[8]; Xu, Ruxiang ^[9]; Liu, Zhi-Jie ^[2]

Chinese Academy of Sciences (CAS), Beijing (China). Inst. of Biophysics. National Lab. of Biomacromolecules; OSTI
Chinese Academy of Sciences (CAS), Beijing (China). Inst. of Biophysics. National Lab. of Biomacromolecules
ShanghaiTech Univ. (China). iHuman Inst.
Chinese Academy of Sciences, Qingdao (China). Qingdao Inst. of Bioenergy and Bioprocess Technology. Shandong Provincial Key Lab. of Energy Genetics
Los Alamos National Lab. (LANL), Los Alamos, NM (United States). Physics Division
Argonne National Lab. (ANL), Argonne, IL (United States). X-ray Science Division
Russian Academy of Sciences, Moscow (Russian Federation). Inst. of Crystallography
Chinese Academy of Sciences (CAS), Beijing (China). Inst. of High Energy Physics. Center for Multi-disciplinary Research
The Military General Hospital of Beijing PLA, Beijing (China). Dept. of Nerosurgery

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 homodimer 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 combination of mutagenesis, biochemical, NMR, and smallangle X-ray scattering (SAXS) techniques. Our results also proved that Uch37 oligomerized in solution and had very low activity against the fluorogenic substrate ubiquitin-7-amino-4-methylcoumarin (Ub-AMC) of de-ubiquitinating enzymes. Uch37Δ^Hb,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 complex. 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.

View Accepted Manuscript (DOE)

Research Organization:: Argonne National Laboratory (ANL), Argonne, IL (United States)

Sponsoring Organization:: Ministry of Health of China; Ministry of Science and Technology of China; National Basic Research Program; National Center for Research Resources; National Institutes of Health (NIH); National Natural Science Foundation of China (NSFC); USDOE Office of Science (SC), Basic Energy Sciences (BES)

Grant/Contract Number:: AC02-05CH11231; AC02-06CH11357

OSTI ID:: 1815417

Journal Information:: Protein & Cell, Journal Name: Protein & Cell Journal Issue: 8 Vol. 5; ISSN 1674-800X

Publisher:: SpringerCopyright Statement

Country of Publication:: United States

Language:: English

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59 BASIC BIOLOGICAL SCIENCES
SAXS analysis
Uch37-Rpn13 complex
de-ubiquitination
iso-peptidase
oligomerization

Mechanism of the Rpn13-induced activation of Uch37

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