A proof-of-concept study in engineering synthetic protein for selective recognition of substrate-free polyubiquitin

doi:10.1002/pmic.201600208

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	A proof-of-concept study in engineering synthetic protein for selective recognition of substrate-free polyubiquitin
	Xiong, Yehui 1; Zeng, Lirong 2; Liu, Wende 1
刊名	PROTEOMICS
	2016
卷号	16 期号:14 页码:1949-1951
关键词	Ubiquitin-binding domain Unanchored polyubiquitin chain Mass spectrometry
ISSN号	1615-9853
DOI	10.1002/pmic.201600208
通讯作者	Xiong, Yehui
英文摘要	Similar to substrate-conjugated polyubiquitin, unanchored polyubiquitin chains are emerging as important regulators for diverse biological processes. The affinity purification of unanchored polyubiquitin from various organisms has been reported, however, tools able to distinguish unanchored polyubiquitin chains with different isopeptide linkages have not yet been described. Toward the goal of selectively identifying and purifying unanchored polyubiquitin chains linked through different Lysines, Scott etal. developed a novel strategy in their study [Proteomics 2016, 16, 1961-1969]. They designed a linker-optimized ubiquitin-binding domain hybrid (t-UBD) containing two UBDs, a ZnFCUBP domain, and a linkage-selective UBA domain, to specifically recognize unanchored Lys48-linked polyubiquitin chains. Subsequently, a series of assays has proved the feasibility of this novel strategy for the purification of endogenous substrate-free Lys48-linked polyubiquitin chains from mammalian cell extracts. Their research not only provides a tool for purifying unanchored polyubiquitin with different isopeptide linkages, but also paves the way for generating reagents to study the function of unanchored polyubiquitin chains of different linkages in the future. The design of UBD hybrids for defined unanchored polyubiquitin (Lys48-polyubiquitin) in this study also set an excellent example for future methodology studies regarding monitoring in vivo dynamic changes in the patterns of ubiquitination.
学科主题	Biochemical Research Methods ; Biochemistry & Molecular Biology
语种	英语
出版者	WILEY-BLACKWELL
WOS记录号	WOS:000380060300001
内容类型	期刊论文
源URL	[http://111.203.20.206/handle/2HMLN22E/11449]
专题	植物保护研究所
作者单位	1.Chinese Acad Agr Sci, Inst Plant Protect, State Key Lab Biol Plant Dis & Insect Pests, Beijing, Peoples R China 2.Univ Nebraska, Dept Plant Pathol, Ctr Plant Sci Innovat, Lincoln, NE 68583 USA
推荐引用方式 GB/T 7714	Xiong, Yehui,Zeng, Lirong,Liu, Wende. A proof-of-concept study in engineering synthetic protein for selective recognition of substrate-free polyubiquitin[J]. PROTEOMICS,2016,16(14):1949-1951.
APA	Xiong, Yehui,Zeng, Lirong,&Liu, Wende.(2016).A proof-of-concept study in engineering synthetic protein for selective recognition of substrate-free polyubiquitin.PROTEOMICS,16(14),1949-1951.
MLA	Xiong, Yehui,et al."A proof-of-concept study in engineering synthetic protein for selective recognition of substrate-free polyubiquitin".PROTEOMICS 16.14(2016):1949-1951.