Cleavage of the C-terminus of NEDD8 by UCH-L3
Cleavage of the C-terminus of NEDD8 by UCH-L3
复制标题
DOI：
10.1006/bbrc.1998.9532
复制
发表时间：
1998-10-29
影响因子：
3.1
通讯作者：
Kamitani, T
中科院分区：
文献类型：
--
作者：
Wada, H;Kito, K;Kamitani, T
NEDD 8是一种新的泛素样蛋白，已被证明以类似于泛素化和sentrinization的方式与核蛋白缀合。为了鉴定参与NEDD 8缀合和去缀合途径的蛋白质，使用酵母双杂交系统以NEDD 8作为诱饵筛选人心脏cDNA文库。发现7个强阳性克隆含有编码泛素C-末端水解酶UCH-L3的cDNA插入片段。体外GST pull-down实验表明UCH-L3与NEDD 8和泛素结合。相比之下，UCH-L3不与sentrin-1、sentrin-2或sentrin-3结合。重组UCH-L3，而不是UCH-L1，能够切割NEDD 8的C-末端。因此，UCH-L3可以作为NEDD 8和泛素的C-末端水解酶发挥作用。UCH-L3可能在NEDD 8的C-末端的切割中发挥生理学上重要的作用，这是NEDD 8与靶蛋白缀合所必需的。(C)北京：科学出版社.
NEDD8 is a novel ubiquitin-like protein that has been shown to conjugate to nuclear proteins in a manner analogous to ubiquitination and sentrinization. To identify proteins that are involved in the NEDD8-conjugation and de-conjugation pathway, the yeast two-hybrid system was used to screen a human heart cDNA library using NEDD8 as a bait. Seven strongly positive clones were found to contain a cDNA insert encoding the ubiquitin C-terminal hydrolase, UCH-L3. In vitro GST pull-down assay demonstrated that UCH-L3 bound to both NEDD8 and ubiquitin. In contrast, UCH-L3 did not bind to sentrin-1, sentrin-2, or sentrin-3. Recombinant UCH-L3, but not UCH-L1, was able to cleave the C-terminus of NEDD8. Thus, UCH-L3 can function as a C-terminal hydrolase for both NEDD8 and ubiquitin. UCH-L3 may play a physiologically significant role in the cleavage of the C-terminus of NEDD8, which is required for NEDD8 to conjugate to target proteins. (C) 1998 Academic Press.