非水解泛素异肽类似物作为去泛素化酶探针。
Nonhydrolyzable ubiquitin-isopeptide isosteres as deubiquitinating enzyme probes.
机构信息
Division of Cell Biology and The Netherlands Proteomics Centre, The Netherlands Cancer Institute, Plesmanlaan 121, 1066 CX Amsterdam, The Netherlands.
出版信息
J Am Chem Soc. 2010 Jul 7;132(26):8834-5. doi: 10.1021/ja101803s.
We demonstrate that oxime ligation is an efficient, straightforward, and generally applicable strategy for generating nonhydrolyzable ubiquitin (Ub)-isopeptide isosteres. We synthesized nonhydrolyzable K48- and K63-linked Ub-isopeptide isosteres to investigate the selectivity of deubiquitinating enzymes for specific linkages employing surface plasmon resonance spectroscopy. The results indicate that deubiquitinating enzymes specifically recognize the local peptide sequence flanking Ub-branched lysine residues in target proteins. The described strategy allows the systematic investigation of sequence requirements for substrate selectivity of deubiquitinating enzymes.
我们证明肟键合是生成不可水解的泛素（Ub）-异肽同系物的有效、直接且通用的策略。我们合成了不可水解的 K48 和 K63 连接的 Ub-异肽同系物，以使用表面等离子体共振光谱法研究去泛素化酶对特定连接的选择性。结果表明，去泛素化酶特异性地识别靶蛋白中 Ub 分支赖氨酸残基侧翼的局部肽序列。所描述的策略允许系统地研究去泛素化酶对底物选择性的序列要求。
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