Ontology highlight
ABSTRACT:
SUBMITTER: Kruger L
PROVIDER: S-EPMC7900238 | biostudies-literature | 2021 Feb
REPOSITORIES: biostudies-literature
Krüger Larissa L Herzberg Christina C Wicke Dennis D Bähre Heike H Heidemann Jana L JL Dickmanns Achim A Schmitt Kerstin K Ficner Ralf R Stülke Jörg J
Nature communications 20210222 1
Many bacteria use cyclic di-AMP as a second messenger to control potassium and osmotic homeostasis. In Bacillus subtilis, several c-di-AMP binding proteins and RNA molecules have been identified. Most of these targets play a role in controlling potassium uptake and export. In addition, c-di-AMP binds to two conserved target proteins of unknown function, DarA and DarB, that exclusively consist of the c-di-AMP binding domain. Here, we investigate the function of the c-di-AMP-binding protein DarB i ...[more]