Article
Differential ubiquitin binding by the acidic loops of Ube2g1 and Ube2r1 enzymes distinguishes their Lys-48-ubiquitylation activities.
The Journal of biological chemistry - 23 Jan 2015
Choi Yun-Seok, Lee Yun-Ju, Lee Seo-Yeon, Shi Lei, Ha Jung-Hye, Cheong Hae-Kap, Cheong Chaejoon, Cohen Robert E, Ryu Kyoung-Seok
Abstract excerpt
The ubiquitin E2 enzymes, Ube2g1 and Ube2r1, are able to synthesize Lys-48-linked polyubiquitins without an E3 ligase but how that is accomplished has been unclear. Although both E2s contain essential acidic loops, only Ube2r1 requires an additional C-terminal extension (184-196) for efficient Lys-48-ubiquitylation activity. The presence of Tyr-102 and Tyr-104 in the Ube2g1 acidic loop enhanced both ubiquitin...
Topics
- Amino Acid Sequence
- Catalytic Domain
- Disulfides
- Esters
- Humans
- Lysine
- Magnetic Resonance Spectroscopy
- Molecular Sequence Data
- Mutation
- Polyubiquitin
- Protein Binding
- Protein Conformation
- Sequence Homology, Amino Acid