FEBS Letters | |
E3 ligase activity of RING finger proteins that interact with Hip‐2, a human ubiquitin‐conjugating enzyme | |
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
【 预 览 】
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RO201912020310802ZK.pdf | 217KB | download |