E3 ligase activity of RING finger proteins that interact with Hip‐2, a human ubiquitin‐conjugating enzyme

FEBS Letters

Lee, Sun-Joo¹  Choi, Ju-Youn²  Kang, Seongman¹  Rhim, Hyangshuk²  Sung, Yong-Mo¹  Park, Hyewon¹ 

[1] Graduate School of Biotechnology, Korea University, Seoul 136-701, South Korea;Research Institute of Molecular Genetics, College of Medicine, Catholic University of Korea, Seoul 137-701, South Korea

关键词: Huntingtin-interacting protein-2;    RING motif;    Ubiquitin-conjugating enzyme;    Ubiquitin ligase;    Yeast two-hybrid;   

DOI  :  10.1016/S0014-5793(01)02689-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

To identify proteins that interact with Huntingtin-interacting protein-2 (Hip-2), a ubiquitin-conjugating enzyme, a yeast two-hybrid screen system was used to isolate five positive clones. Sequence analyses showed that, with one exception, all Hip-2-interacting proteins contained the RING finger motifs. The interaction of Hip-2 with RNF2, one of the clones, was further confirmed through in vitro and in vivo experiments. Mutations in the RING domain of RNF2 prevented the clone from binding to Hip-2, an indication that the RING domain is the binding determinant. RNF2 showed a ubiquitin ligase (E3) activity in the presence of Hip-2, suggesting that a subset of RING finger proteins may have roles as E3s.

【 授权许可】

Unknown