Ontology highlight
ABSTRACT:
SUBMITTER: Yu C
PROVIDER: S-EPMC4686759 | biostudies-literature | 2015 Dec
REPOSITORIES: biostudies-literature
Yu Clinton C Mao Haibin H Novitsky Eric J EJ Tang Xiaobo X Rychnovsky Scott D SD Zheng Ning N Huang Lan L
Nature communications 20151203
The full enzymatic activity of the cullin-RING ubiquitin ligases (CRLs) requires a ubiquitin-like protein (that is, Nedd8) modification. By deamidating Gln40 of Nedd8 to glutamate (Q40E), the bacterial cycle-inhibiting factor (Cif) family is able to inhibit CRL E3 activities, thereby interfering with cellular functions. Despite extensive structural studies on CRLs, the molecular mechanism by which Nedd8 Gln40 deamidation affects CRL functions remains unclear. We apply a new quantitative cross-li ...[more]