Identification of NEDD8-conjugation site in human cullin-2

被引:75
作者
Wada, H
Yeh, ETH
Kamitani, T
机构
[1] Univ Texas, Hlth Sci Ctr, Dept Internal Med, Div Mol Med, Houston, TX 77030 USA
[2] Univ Texas, Hlth Sci Ctr, Inst Mol Med Prevent Human Dis, Res Ctr Cardiovasc Dis, Houston, TX 77030 USA
关键词
D O I
10.1006/bbrc.1999.0339
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
NEDD8 is a novel ubiquitin-like protein that has been shown to conjugate to nuclear proteins in a manner analogous to ubiquitination and sentrinization. Recently, human cullin-4A was reported to be conjugated by a single molecule of NEDD8. Here, we show that human cullin-2 is also conjugated by a single molecule of the NEDD8. The C-terminal 171-amino-acid residues in human cullin-2 are sufficient for NEDD8-conjugation. In addition, the equivalent C-terminal fragments of other cullins have been shown to be conjugated by NEDD8. Mapping of the NEDD8-conjugation site revealed that Lys-689 in human cullin-2 is conjugated by NEDD8. Interestingly, the Lys residue at position 689 in cullin-2 is conserved in all cullin family members, including human cullin-1, -2, -3, -4A, -4B, and -5 and yeast cullin (Cdc53), suggesting the possibility that other cullin family members are conjugated by NEDD8/Rub1 at a Lys residue of equivalent position. (C) 1999 Academic Press.
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页码:100 / 105
页数:6
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