A cyclic GMP-dependent signalling pathway regulates bacterial phytopathogenesis

TY - JOUR

T1 - A cyclic GMP-dependent signalling pathway regulates bacterial phytopathogenesis

AU - An, Shi-Qi

AU - Chin, Ko-Hsin

AU - Febrer, Melanie

AU - McCarthy, Yvonne

AU - Yang, Jauo-Guey

AU - Liu, Chung-Liang

AU - Swarbreck, David

AU - Rogers, Jane

AU - Dow, J. Maxwell

AU - Chou, Shan-Ho

AU - Ryan, Robert P

PY - 2013/9/11

Y1 - 2013/9/11

N2 - Cyclic guanosine 3',5'-monophosphate (cyclic GMP) is a second messenger whose role in bacterial signalling is poorly understood. A genetic screen in the plant pathogen Xanthomonas campestris (Xcc) identified that XC_0250, which encodes a protein with a class III nucleotidyl cyclase domain, is required for cyclic GMP synthesis. Purified XC_0250 was active in cyclic GMP synthesis in vitro. The linked gene XC_0249 encodes a protein with a cyclic mononucleotide-binding (cNMP) domain and a GGDEF diguanylate cyclase domain. The activity of XC_0249 in cyclic di-GMP synthesis was enhanced by addition of cyclic GMP. The isolated cNMP domain of XC_0249 bound cyclic GMP and a structure-function analysis, directed by determination of the crystal structure of the holo-complex, demonstrated the site of cyclic GMP binding that modulates cyclic di-GMP synthesis. Mutation of either XC_0250 or XC_0249 led to a reduced virulence to plants and reduced biofilm formation in vitro. These findings describe a regulatory pathway in which cyclic GMP regulates virulence and biofilm formation through interaction with a novel effector that directly links cyclic GMP and cyclic di-GMP signalling.

AB - Cyclic guanosine 3',5'-monophosphate (cyclic GMP) is a second messenger whose role in bacterial signalling is poorly understood. A genetic screen in the plant pathogen Xanthomonas campestris (Xcc) identified that XC_0250, which encodes a protein with a class III nucleotidyl cyclase domain, is required for cyclic GMP synthesis. Purified XC_0250 was active in cyclic GMP synthesis in vitro. The linked gene XC_0249 encodes a protein with a cyclic mononucleotide-binding (cNMP) domain and a GGDEF diguanylate cyclase domain. The activity of XC_0249 in cyclic di-GMP synthesis was enhanced by addition of cyclic GMP. The isolated cNMP domain of XC_0249 bound cyclic GMP and a structure-function analysis, directed by determination of the crystal structure of the holo-complex, demonstrated the site of cyclic GMP binding that modulates cyclic di-GMP synthesis. Mutation of either XC_0250 or XC_0249 led to a reduced virulence to plants and reduced biofilm formation in vitro. These findings describe a regulatory pathway in which cyclic GMP regulates virulence and biofilm formation through interaction with a novel effector that directly links cyclic GMP and cyclic di-GMP signalling.

UR - https://www.scopus.com/pages/publications/84884292053

U2 - 10.1038/emboj.2013.165

DO - 10.1038/emboj.2013.165

M3 - Article

C2 - 23881098

SN - 0261-4189

VL - 32

SP - 2430

EP - 2438

JO - EMBO Journal

JF - EMBO Journal

IS - 18

ER -