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Publication Abstract from PubMed

Cyclic di-AMP is an essential signalling molecule in Gram-positive bacteria. This second messenger regulates the osmotic pressure of the cell by interacting directly with the regulatory domains, either RCK_C or CBS domains, of several potassium and osmolyte uptake membrane protein systems. Cyclic di-AMP also targets stand-alone CBS domain proteins such as DarB in Bacillus subtilis and CbpB in Listeria monocytogenes. We show here that the CbpB protein of Group B Streptococcus binds c-di-AMP with a very high affinity. Crystal structures of CbpB reveal the determinants of binding specificity and significant conformational changes occurring upon c-di-AMP binding. Deletion of the cbpB gene alters bacterial growth in low potassium conditions most likely due to a decrease in the amount of ppGpp caused by a loss of interaction between CbpB and Rel, the GTP/GDP pyrophosphokinase.

The c-di-AMP-binding protein CbpB modulates the level of ppGpp alarmone in Streptococcus agalactiae.,Covaleda-Cortes G, Mechaly A, Brissac T, Baehre H, Devaux L, England P, Raynal B, Hoos S, Gominet M, Firon A, Trieu-Cuot P, Kaminski PA FEBS J. 2023 Jan 11. doi: 10.1111/febs.16724. PMID:36629470^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.