A proof-of-concept study in engineering synthetic protein for selective recognition of substrate-free polyubiquitin | |
Xiong, Yehui1; Zeng, Lirong2; Liu, Wende1 | |
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. |
个性服务 |
查看访问统计 |
相关权益政策 |
暂无数据 |
收藏/分享 |
除非特别说明,本系统中所有内容都受版权保护,并保留所有权利。
修改评论