Artikel ; Online: Cyclic-di-GMP binds to histidine kinase RavS to control RavS-RavR phosphotransfer and regulates the bacterial lifestyle transition between virulence and swimming.
2019 Band 15, Heft 8, Seite(n) e1007952
Abstract: The two-component signalling system (TCS) comprising a histidine kinase (HK) and a response regulator (RR) is the predominant bacterial sense-and-response machinery. Because bacterial cells usually encode a number of TCSs to adapt to various ecological ... ...
Abstract | The two-component signalling system (TCS) comprising a histidine kinase (HK) and a response regulator (RR) is the predominant bacterial sense-and-response machinery. Because bacterial cells usually encode a number of TCSs to adapt to various ecological niches, the specificity of a TCS is in the centre of regulation. Specificity of TCS is defined by the capability and velocity of phosphoryl transfer between a cognate HK and a RR. Here, we provide genetic, enzymology and structural data demonstrating that the second messenger cyclic-di-GMP physically and specifically binds to RavS, a HK of the phytopathogenic, gram-negative bacterium Xanthomonas campestris pv. campestris. The [c-di-GMP]-RavS interaction substantially promotes specificity between RavS and RavR, a GGDEF-EAL domain-containing RR, by reinforcing the kinetic preference of RavS to phosphorylate RavR. [c-di-GMP]-RavS binding effectively decreases the phosphorylation level of RavS and negatively regulates bacterial swimming. Intriguingly, the EAL domain of RavR counteracts the above regulation by degrading c-di-GMP and then increasing the level of phosphorylated RavS. Therefore, RavR acts as a bifunctional phosphate sink that finely controls the level of phosphorylated RavS. These biochemical processes interactively modulate the phosphoryl flux between RavS-RavR and bacterial lifestyle transition. Our results revealed that c-di-GMP acts as an allosteric effector to dynamically modulate specificity between HK and RR. |
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Mesh-Begriff(e) | Bacterial Proteins/genetics ; Bacterial Proteins/metabolism ; Biofilms/growth & development ; Cyclic GMP/analogs & derivatives ; Cyclic GMP/metabolism ; Flagella/physiology ; Gene Expression Regulation, Bacterial ; Histidine Kinase/genetics ; Histidine Kinase/metabolism ; Phosphorylation ; Signal Transduction ; Virulence/physiology ; Xanthomonas campestris/genetics ; Xanthomonas campestris/growth & development ; Xanthomonas campestris/metabolism |
Chemische Substanzen | Bacterial Proteins ; bis(3',5')-cyclic diguanylic acid (61093-23-0) ; Histidine Kinase (EC 2.7.13.1) ; Cyclic GMP (H2D2X058MU) |
Sprache | Englisch |
Erscheinungsdatum | 2019-08-13 |
Erscheinungsland | United States |
Dokumenttyp | Journal Article ; Research Support, Non-U.S. Gov't |
ZDB-ID | 2205412-1 |
ISSN | 1553-7374 ; 1553-7366 |
ISSN (online) | 1553-7374 |
ISSN | 1553-7366 |
DOI | 10.1371/journal.ppat.1007952 |
Datenquelle | MEDical Literature Analysis and Retrieval System OnLINE |
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