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

FEBS Letters

Bte Mustafa, Fatimah¹  Yang, Hongyuan¹  Li, Tianwei¹  Teo, Tian-Seng¹  Lee, Mui-Khin¹  Duan, Wei¹  Lee, Boon-Heng¹ 

[1] Department of Biochemistry, Faculty of Medicine, National University of Singapore, 10 Kent Ridge Crescent, 119260 Singapore, Singapore

关键词: Ubiquitin C-terminal hydrolase;    Isopeptidase;    Ubiquitin;    Yeast two-hybrid system;    UCH;    ubiquitin C-terminal hydrolase;    UIP1;    UCH37 interacting protein 1;    GST;    glutathione-S-transferase;    ORF;    open reading frame;    RT-PCR;    reverse transcription-polymerase chain reaction;    G3PDH;    glyceraldehyde-3-phosphate dehydrogenase;    IPTG;    isopropyl-β-D-thiogalactopyranoside;    PMSF;    phenylmethylsulfonyl fluoride;    DTT;    dithiothreitol;    HRP;    horseradish peroxidase;   

DOI  :  10.1016/S0014-5793(00)02436-4

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 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 1). The interaction of UCH37 with S14 or UIP1 was confirmed by in vitro binding assay and in vivo co-immunoprecipitation 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.

【 授权许可】

Unknown