Regulation of (p)ppGpp hydrolysis by a conserved archetypal regulatory domain

Séverin Ronneau, Julien Caballero-Montes, Jérôme Coppine, Aurélie Mayard, Abel Garcia-Pino, Régis Hallez

Résultats de recherche: Contribution à un journal/une revueArticle

Résumé

Sensory and regulatory domains allow bacteria to adequately respond to environmental changes. The regulatory ACT (Aspartokinase, Chorismate mutase and TyrA) domains are mainly found in metabolic-related proteins as well as in long (p)ppGpp synthetase/hydrolase enzymes. Here, we investigate the functional role of the ACT domain of SpoT, the only (p)ppGpp synthetase/hydrolase of Caulobacter crescentus. We show that SpoT requires the ACT domain to efficiently hydrolyze (p)ppGpp. In addition, our in vivo and in vitro data show that the phosphorylated version of EIIANtr (EIIANtr∼P) interacts directly with the ACT and inhibits the hydrolase activity of SpoT. Finally, we highlight the conservation of the ACT-dependent interaction between EIIANtr∼P and SpoT/Rel along with the phosphotransferase system (PTSNtr)-dependent regulation of (p)ppGpp accumulation upon nitrogen starvation in Sinorhizobium meliloti, a plant-associated α-proteobacterium. Thus, this work suggests that α-proteobacteria might have inherited from a common ancestor, a PTSNtr dedicated to modulate (p)ppGpp levels in response to nitrogen availability.
langue originaleAnglais
Pages (de - à)843-854
Nombre de pages12
journalNucleic Acids Research
Volume47
Numéro de publication2
Les DOIs
étatPublié - 25 janv. 2019

    Empreinte digitale

Contient cette citation