Bacterial cyclic diguanylate signaling networks sense temperature
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Author list: Almblad H., Randall T.E., Liu F., Leblanc K., Groves R.A., Kittichotirat W., Winsor G.L., Fournier N., Au E., Groizeleau J., Rich J.D., Lou Y., Granton E., Jennings L.K., Singletary L.A., Winstone T.M.L., Good N.M., Bumgarner R.E., Hynes M.F., Singh M., Stietz M.S., Brinkman F.S.L., Kumar A., Brassinga A.K.C., Parsek M.R., Tseng B.S., Lewis I.A., Yipp B.G., MacCallum J.L., Harrison J.J.
Publisher: Nature Research
Publication year: 2021
Journal: Nature Communications (2041-1723)
Volume number: 12
Issue number: 1
Start page: 1
End page: 14
Number of pages: 14
ISSN: 2041-1723
eISSN: 2041-1723
Languages: English-Great Britain (EN-GB)
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Abstract
Many bacteria use the second messenger cyclic diguanylate (c-di-GMP) to control motility, biofilm production and virulence. Here, we identify a thermosensory diguanylate cyclase (TdcA) that modulates temperature-dependent motility, biofilm development and virulence in the opportunistic pathogen Pseudomonas aeruginosa. TdcA synthesizes c-di-GMP with catalytic rates that increase more than a hundred-fold over a ten-degree Celsius change. Analyses using protein chimeras indicate that heat-sensing is mediated by a thermosensitive Per-Arnt-SIM (PAS) domain. TdcA homologs are widespread in sequence databases, and a distantly related, heterologously expressed homolog from the Betaproteobacteria order Gallionellales also displayed thermosensitive diguanylate cyclase activity. We propose, therefore, that thermotransduction is a conserved function of c-di-GMP signaling networks, and that thermosensitive catalysis of a second messenger constitutes a mechanism for thermal sensing in bacteria. © 2021, The Author(s).
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