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A rendezvous of two second messengers: The c-di-AMP receptor protein DarB controls (p)ppGpp synthesis in Bacillus subtilis

ABSTRACT: DarB is a cyclic di-AMP binding protein consisting of two CBS (Cystathionine-beta synthase) domains. To reveal the global role of the second-messenger, understanding the function of the receptor proteins is fundamental. In order to do so, we aimed to identify potential binding partners of DarB in vitro with an unbiased protein pulldown experiment. In this study, we identified the (p)ppGpp synthetase/ hydrolase RelA as the binding partner of DarB and could confirm these findings with an in vivo interaction experiment.

INSTRUMENT(S): LTQ Orbitrap Velos, Q Exactive

ORGANISM(S): Bacillus Subtilis Subsp. Subtilis Str. 168

SUBMITTER: Oliver Valerius

LAB HEAD: Jörg Stülke

PROVIDER: PXD018087 | Pride | 2021-01-12

REPOSITORIES: Pride

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A meet-up of two second messengers: the c-di-AMP receptor DarB controls (p)ppGpp synthesis in Bacillus subtilis.

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]

PMID: 33619274

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