Chemical Synthesis of Ubiquitinated Peptides with Varying Lengths and Types of Ubiquitin Chains to Explore the Activity of Deubiquitinases

被引:92
作者
Bavikar, Sudhir N. [1 ,2 ]
Spasser, Liat [1 ,2 ]
Haj-Yahya, Mahmood [1 ,2 ]
Karthikeyan, Subramanian Vedhanarayanan [1 ,2 ]
Moyal, Tal [1 ,2 ]
Kumar, K. S. Ajish [1 ,2 ]
Brik, Ashraf [1 ,2 ]
机构
[1] Ben Gurion Univ Negev, Dept Chem, IL-84105 Beer Sheva, Israel
[2] Ben Gurion Univ Negev, Natl Inst Biotechnol Negev, IL-84105 Beer Sheva, Israel
基金
以色列科学基金会;
关键词
peptide ligations; protein modifications; protein synthesis; solid-phase synthesis; ubiquitin; CARBOXYL-TERMINAL HYDROLASE; RECOMBINANT PROTEINS; POLYUBIQUITIN CHAINS; CRYSTAL-STRUCTURE; STRUCTURAL BASIS; UBIQUITYLATION; DIUBIQUITIN; SUBSTRATE; LIGATION; DEGRADATION;
D O I
10.1002/anie.201106430
中图分类号
O6 [化学];
学科分类号
070301 [无机化学];
摘要
Adding one at a time: A general and effective synthesis yields a peptide attached to mono-, di-, tri-, and tetraubiquitin (Ub) chains (see picture for peptides with Ub and Ub 4), linked through lysine residues K48 or K63. These sets of ubiquitinated peptides were prepared in good quantities, and the activity of the enzymes UCH-L3 and IsoT with these different substrates was studied. Copyright © 2012 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim.
引用
收藏
页码:758 / 763
页数:6
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