Format

Send to

Choose Destination
J Bacteriol. 2018 Sep 17. pii: JB.00462-18. doi: 10.1128/JB.00462-18. [Epub ahead of print]

Making and breaking of an essential poison: the cyclases and phosphodiesterases that produce and degrade the essential second messenger cyclic di-AMP in bacteria.

Author information

1
Department of General Microbiology and Department of Molecular Structural Biology, Institute of Microbiology and Genetics, GZMB, Georg-August University Göttingen, Germany.
2
Department of General Microbiology and Department of Molecular Structural Biology, Institute of Microbiology and Genetics, GZMB, Georg-August University Göttingen, Germany. jstuelk@gwdg.de.

Abstract

Cyclic di-AMP is a second messenger nucleotide that is produced by many bacteria and some archaea. Recent work has shown that c-di-AMP is unique among the signaling nucleotides, as this molecule is in many bacteria both essential on one hand and toxic upon accumulation on the other. Moreover, in bacteria like Bacillus subtilis, c-di-AMP controls a biological process, potassium homeostasis, by binding both potassium transporters and riboswitch molecules in the mRNAs that encode the potassium transporters. In addition to the control of potassium homeostasis, c-di-AMP has been implicated in many cellular activities including DNA repair, cell wall homeostasis, osmotic adaptation, biofilm formation, central metabolism, and virulence. C-di-AMP is synthesized and degraded by diadenylate cyclases and phosphodiesterases, respectively. In the diadenylate cyclases, one type of catalytic domain, the DAC domain, is coupled to various other domains that control the localization, the protein-protein interactions, and the regulation of the enzymes. The phosphodiesterases have a catalytic core that consists either of a DHH/DHHA1 or of a HD domain. Recent findings on the occurrence, domain organization, activity control and structural features of diadenylate cyclases and phosphodiesterases are discussed in this review.

PMID:
30224435
DOI:
10.1128/JB.00462-18

Supplemental Content

Full text links

Icon for HighWire
Loading ...
Support Center