AI Article Synopsis
- Cyclic di-AMP is crucial for Gram-positive bacteria, helping to regulate osmotic pressure by interacting with specific protein domains related to potassium and osmolyte uptake.
- The CbpB protein from Group B Streptococcus has a strong binding affinity for c-di-AMP, and its crystal structure reveals how it recognizes c-di-AMP and undergoes significant changes when binding occurs.
- Deleting the cbpB gene negatively impacts bacterial growth under low potassium conditions, likely due to reduced levels of ppGpp resulting from disrupted interaction between CbpB and the enzyme Rel.
Article Abstract
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.
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