Identification of two proteins, S14 and UIP1, that interact with UCH37

被引：19

作者：

Li, TW ^{[1
]}

Duan, W ^{[1
]}

Yang, HY ^{[1
]}

Lee, MK ^{[1
]}

Mustafa, FB ^{[1
]}

Lee, BH ^{[1
]}

Teo, TS ^{[1
]}

机构：

[1] Natl Univ Singapore, Fac Med, Dept Biochem, Singapore 119260, Singapore

来源：

FEBS LETTERS | 2001年 / 488卷 / 03期

关键词：

ubiquitin C-terminal hydrolase; isopeptidase; ubiquitin; yeast two-hybrid system;

D O I：

10.1016/S0014-5793(00)02436-4

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：

By the use of the yeast two-hybrid screen we have identified two proteins that interacted with UCH37: S14, which is a subunit of PA700 and a novel protein, UIP1 (UCH37 interacting protein I). The interaction of UCH37 with S14 or UIP1 was confirmed by in vitro binding assay and in vivo coimmunoprecipitation analysis. The C-terminal extension of UCH37 is essential for interaction with S14 or UIP1 as shown by the yeast two-hybrid assay and the in vitro binding assay. Furthermore, UIP1 blocked the interaction between UCH37 and S14 in vitro. (C) 2001 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.

引用

页码：201 / 205

页数：5

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