Too much of a good thing: regulated depletion of c-di-AMP in the bacterial cytoplasm.

Too much of a good thing: regulated depletion of c-di-AMP in the bacterial cytoplasm.
Curr Opin Microbiol. 2016 Jan 7;30:22-29
Authors: Huynh TN, Woodward JJ
Abstract
Bacteria that synthesize c-di-AMP also encode several mechanisms for controlling c-di-AMP levels within the cytoplasm. One major class of phosphodiesterases comprises GdpP and DhhP homologs, which degrade c-di-AMP into the linear molecule 5'-pApA or AMP by the DHH-DHHA1 domain. The other major class comprises PgpH homologs, which degrade c-di-AMP by the HD domain. Both GdpP and PgpH harbor sensory domains, likely to regulate c-di-AMP hydrolysis activity in response to signal input. As another possible mechanism for controlling cytoplasmic c-di-AMP levels, bacteria also secrete c-di-AMP via multidrug resistance transporters, as demonstrated for Listeria monocytogenes. Mutants that accumulate high c-di-AMP levels, by deletion of phosphodiesterases or multidrug resistance transporters, exhibit aberrant physiology, growth defects, and attenuated virulence in infection.
PMID: 26773214 [PubMed - as supplied by publisher]

Source: Current Opinion in Microbiology - January 7, 2016 Category: Microbiology Authors: Huynh TN, Woodward JJ Tags: Curr Opin Microbiol Source Type: research