Ontology highlight
ABSTRACT:
SUBMITTER: Bijlmakers MJ
PROVIDER: S-EPMC4944129 | biostudies-literature | 2016 Jul
REPOSITORIES: biostudies-literature
Bijlmakers Marie-José MJ Teixeira João M C JM Boer Roeland R Mayzel Maxim M Puig-Sàrries Pilar P Karlsson Göran G Coll Miquel M Pons Miquel M Crosas Bernat B
Scientific reports 20160714
The activity of RING ubiquitin ligases (E3s) depends on an interaction between the RING domain and ubiquitin conjugating enzymes (E2), but posttranslational events or additional structural elements, yet largely undefined, are frequently required to enhance or regulate activity. Here, we show for the ubiquitin ligase RNF125 that, in addition to the RING domain, a C2HC Zn finger (ZnF) is crucial for activity, and a short linker sequence (Li2(120-128)) enhances activity. The contribution of these r ...[more]