期刊
NATURE STRUCTURAL & MOLECULAR BIOLOGY
卷 22, 期 12, 页码 959-967出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.3114
关键词
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资金
- Max Planck Society
- Deutsche Forschungsgemeinschaft [DFG-SPP1365 PI 917/2-1, DEG-SPP1365]
- Academy of Finland [251133]
- Sigrid Juselius Foundation
- COST [BM1307]
- Academy of Finland (AKA) [251133, 251133] Funding Source: Academy of Finland (AKA)
SUMO chains act as stress-induced degradation tags or repair factor-recruiting signals at DNA lesions. Although El activating, E2 conjugating and E3 ligating enzymes efficiently assemble SUMO chains, specific chain-elongation mechanisms are unknown. E4 elongases are specialized E3 ligases that extend a chain but are inefficient in the initial conjugation of the modifier. We identified ZNF451, a representative member of a new class of SUMO2 and SUM03 (SUMO2/3)-specific enzymes that execute catalysis via a tandem SUMO-interaction motif (SIM) region. One SIM positions the donor SUMO while a second SIM binds SUMO on the back side of the E2 enzyme. This tandem-SIM region is sufficient to extend a back side-anchored SUMO chain (E4 elongase activity), whereas efficient chain initiation also requires a zinc-finger region to recruit the initial acceptor SUMO (E3 ligase activity). Finally, we describe four human proteins sharing E4 elongase activities and their function in stress-induced SUMO2/3 conjugation.
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