TY - JOUR
T1 - Bacterial cyclic diguanylate signaling networks sense temperature
AU - Almblad, Henrik
AU - Randall, Trevor E.
AU - Liu, Fanny
AU - Leblanc, Katherine
AU - Groves, Ryan A.
AU - Kittichotirat, Weerayuth
AU - Winsor, Geoffrey L.
AU - Fournier, Nicolas
AU - Au, Emily
AU - Groizeleau, Julie
AU - Rich, Jacquelyn D.
AU - Lou, Yuefei
AU - Granton, Elise
AU - Jennings, Laura K.
AU - Singletary, Larissa A.
AU - Winstone, Tara M.L.
AU - Good, Nathan M.
AU - Bumgarner, Roger E.
AU - Hynes, Michael F.
AU - Singh, Manu
AU - Stietz, Maria Silvina
AU - Brinkman, Fiona S.L.
AU - Kumar, Ayush
AU - Brassinga, Ann Karen Cornelia
AU - Parsek, Matthew R.
AU - Tseng, Boo Shan
AU - Lewis, Ian A.
AU - Yipp, Bryan G.
AU - MacCallum, Justin L.
AU - Harrison, Joe Jonathan
N1 - Publisher Copyright:
© 2021, The Author(s).
PY - 2021/12/1
Y1 - 2021/12/1
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=85103745747&partnerID=8YFLogxK
U2 - 10.1038/s41467-021-22176-2
DO - 10.1038/s41467-021-22176-2
M3 - Article
C2 - 33790266
AN - SCOPUS:85103745747
SN - 2041-1723
VL - 12
JO - Nature Communications
JF - Nature Communications
IS - 1
M1 - 1986
ER -