Ontology highlight
ABSTRACT:
SUBMITTER: Castro-Roa D
PROVIDER: S-EPMC3836179 | biostudies-other | 2013 Dec
REPOSITORIES: biostudies-other
Castro-Roa Daniel D Garcia-Pino Abel A De Gieter Steven S van Nuland Nico A J NAJ Loris Remy R Zenkin Nikolay N
Nature chemical biology 20131020 12
Fic proteins are ubiquitous in all of the domains of life and have critical roles in multiple cellular processes through AMPylation of (transfer of AMP to) target proteins. Doc from the doc-phd toxin-antitoxin module is a member of the Fic family and inhibits bacterial translation by an unknown mechanism. Here we show that, in contrast to having AMPylating activity, Doc is a new type of kinase that inhibits bacterial translation by phosphorylating the conserved threonine (Thr382) of the translat ...[more]