Structural Basis for Ubiquitin Recognition by a Novel Domain from Human Phospholipase A(2)-activating Protein

doi:10.1074/jbc.M109.009126

	Structural Basis for Ubiquitin Recognition by a Novel Domain from Human Phospholipase A(2)-activating Protein
	Fu, Qing-Shan 1,3; Zhou, Chen-Jie 1; Gao, Hong-Chang 2; Jiang, Ya-Jun 1,3; Zhou, Zi-Ren 1,3; Hong, Jing 2; Yao, Wen-Ming 2; Song, Ai-Xin 1; Lin, Dong-Hai 2; Hu, Hong-Yu 1
刊名	JOURNAL OF BIOLOGICAL CHEMISTRY
	2009-07-10
卷号	284 期号:28 页码:19043-19052
ISSN号	0021-9258
DOI	10.1074/jbc.M109.009126
文献子类	Article
英文摘要	Ubiquitin (Ub) is an essential modifier conserved in all eukaryotes from yeast to human. Phospholipase A(2)-activating protein (PLAA), a mammalian homolog of yeast DOA1/UFD3, has been proposed to be able to bind with Ub, which plays important roles in endoplasmic reticulum-associated degradation, vesicle formation, and DNA damage response. We have identified a core domain from the PLAA family ubiquitin-binding region of human PLAA (residues 386-465, namely PFUC) that can bind Ub and elucidated its solution structure and Ub-binding mode by NMR approaches. The PFUC domain possesses equal population of two conformers in solution by cis/trans-isomerization, whereas the two isomers exhibit almost equivalent Ub binding abilities. This domain structure takes a novel fold consisting of four beta-strands and two alpha-helices, and the Ub-binding site on PFUC locates in the surface of alpha 2-helix, which is to some extent analogous to those of UBA, CUE, and UIM domains. This study provides structural basis and biochemical information for Ub recognition of the novel PFU domain from a PLAA family protein that may connect ubiquitination and degradation in endoplasmic reticulum-associated degradation.
资助项目	National Basic Research Program of China[2006CB910305] ; National Basic Research Program of China[2006CB806508] ; National Basic Research Program of China[2007CB914304] ; National Natural Science Foundation of China[30600103] ; National Natural Science Foundation of China[30670431]
WOS关键词	INTERACTING MOTIF ; CHEMICAL-SHIFT ; SACCHAROMYCES-CEREVISIAE ; CRYSTAL-STRUCTURE ; BINDING DOMAINS ; COMPLEX REVEALS ; PROTEASOME ; ERAD ; NMR ; S5A
WOS研究方向	Biochemistry & Molecular Biology
语种	英语
出版者	AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
WOS记录号	WOS:000267711500053
内容类型	期刊论文
源URL	[http://119.78.100.183/handle/2S10ELR8/279185]
专题	分析化学研究室
通讯作者	Lin, Dong-Hai
作者单位	1.Chinese Acad Sci, State Key Lab Mol Biol, Inst Biochem & Cell Biol, Shanghai Inst Biol Sci, Shanghai 200031, Peoples R China; 2.Chinese Acad Sci, Shanghai Inst Mat Med, Shanghai Inst Biol Sci, Shanghai 201203, Peoples R China; 3.Chinese Acad Sci, Grad Sch, Beijing 100039, Peoples R China
推荐引用方式 GB/T 7714	Fu, Qing-Shan,Zhou, Chen-Jie,Gao, Hong-Chang,et al. Structural Basis for Ubiquitin Recognition by a Novel Domain from Human Phospholipase A(2)-activating Protein[J]. JOURNAL OF BIOLOGICAL CHEMISTRY,2009,284(28):19043-19052.
APA	Fu, Qing-Shan.,Zhou, Chen-Jie.,Gao, Hong-Chang.,Jiang, Ya-Jun.,Zhou, Zi-Ren.,...&Hu, Hong-Yu.(2009).Structural Basis for Ubiquitin Recognition by a Novel Domain from Human Phospholipase A(2)-activating Protein.JOURNAL OF BIOLOGICAL CHEMISTRY,284(28),19043-19052.
MLA	Fu, Qing-Shan,et al."Structural Basis for Ubiquitin Recognition by a Novel Domain from Human Phospholipase A(2)-activating Protein".JOURNAL OF BIOLOGICAL CHEMISTRY 284.28(2009):19043-19052.