Solution Structure of Yeast Rpn9 INSIGHTS INTO PROTEASOME LID ASSEMBLY

doi:10.1074/jbc.M114.626762

CORC > 北京大学 > 化学与分子工程学院

	Solution Structure of Yeast Rpn9 INSIGHTS INTO PROTEASOME LID ASSEMBLY
	Hu, Yunfei ; Wu, Yujie ; Li, Qianwen ; Zhang, Wenbo ; Jin, Changwen
刊名	journal of biological chemistry
	2015
关键词	N-15 RESONANCE ASSIGNMENTS RESIDUAL DIPOLAR COUPLINGS TORSION ANGLE DYNAMICS 26S PROTEASOME SACCHAROMYCES-CEREVISIAE REGULATORY PARTICLE CRYSTAL-STRUCTURE 20S PROTEASOME ELECTRON-MICROSCOPY MOLECULAR-DYNAMICS
DOI	10.1074/jbc.M114.626762
英文摘要	The regulatory particle (RP) of the 26 S proteasome functions in preparing polyubiquitinated substrates for degradation. The lid complex of the RP contains an Rpn8-Rpn11 heterodimer surrounded by a horseshoe-shaped scaffold formed by six proteasome-COP9/CSN-initiation factor (PCI)-containing subunits. The PCI domains are essential for lid assembly, whereas the detailed molecular mechanisms remain elusive. Recent cryo-EM studies at near-atomic resolution provided invaluable information on the RP architecture in different functional states. Nevertheless, atomic resolution structural information on the RP is still limited, and deeper understanding of RP assembly mechanism requires further studies on the structures and interactions of individual subunits or subcomplexes. Herein we report the high-resolution NMR structures of the PCI-containing subunit Rpn9 from Saccharomyces cerevisiae. The 45-kDa protein contains an all-helical N-terminal domain and a (-terminal PCI domain linked via a semiflexible hinge. The N-terminal domain mediates interaction with the ubiquitin receptor Rpn10, whereas the PCI domain mediates interaction with the neighboring PCI subunit Rpn5. The Rpn9-Rpn5 interface highlights two structural motifs on the winged helix module forming a hydrophobic center surrounded by ionic pairs, which is a common pattern for all PCI-PCI interactions in the lid. The results suggest that divergence in surface composition among different PCI pairs may contribute to the modulation of lid assembly.; Biochemistry & Molecular Biology; SCI(E); EI; PubMed; 0; ARTICLE; changwen@pku.edu.cn; 11; 6878-6889; 290
语种	英语
内容类型	期刊论文
源URL	[http://ir.pku.edu.cn/handle/20.500.11897/312539]
专题	化学与分子工程学院生命科学学院
推荐引用方式 GB/T 7714	Hu, Yunfei,Wu, Yujie,Li, Qianwen,et al. Solution Structure of Yeast Rpn9 INSIGHTS INTO PROTEASOME LID ASSEMBLY[J]. journal of biological chemistry,2015.
APA	Hu, Yunfei,Wu, Yujie,Li, Qianwen,Zhang, Wenbo,&Jin, Changwen.(2015).Solution Structure of Yeast Rpn9 INSIGHTS INTO PROTEASOME LID ASSEMBLY.journal of biological chemistry.
MLA	Hu, Yunfei,et al."Solution Structure of Yeast Rpn9 INSIGHTS INTO PROTEASOME LID ASSEMBLY".journal of biological chemistry (2015).