TY - JOUR
T1 - An Arabidopsis thaliana leucine-rich repeat protein harbors an adenylyl cyclase catalytic center and affects responses to pathogens
AU - Bianchet, Chantal
AU - Wong, Aloysius Tze
AU - Quaglia, Mara
AU - Alquraishi, May Majed
AU - Gehring, Christoph A
AU - Ntoukakis, Vardis
AU - Pasqualini, Stefania
N1 - KAUST Repository Item: Exported on 2020-10-01
Acknowledgements: This project was funded by King Abdullah University of Science and Technology, Royal Society, Biotechnology and Biological Science Research Council grants (BB/L019345/1 and BB/M017982/1) and “Fondo di Ateneo per la Ricerca di Base 2015” financed by University of Perugia. We are grateful to Aleš Lebeda and Božena Sedláková (Palacký University, Olomouc) for providing the Golovinomyces orontii isolates. AW is supported by grants from the National Natural Science Foundation of China (31850410470) and the Zhejiang Provincial Natural Science Foundation of China (Q19C130001).
PY - 2018/11/3
Y1 - 2018/11/3
N2 - Adenylyl cyclases (ACs) catalyze the formation of the second messenger cAMP from ATP. Here we report the characterization of an Arabidopsis thaliana leucine-rich repeat (LRR) protein (At3g14460; AtLRRAC1) as an adenylyl cyclase. Using an AC-specific search motif supported by computational assessments of protein models we identify an AC catalytic center within the N-terminus and demonstrate that AtLRRAC1 can generate cAMP in vitro. Knock-out mutants of AtLRRAC1 have compromised immune responses to the biotrophic fungus Golovinomyces orontii and the hemibiotrophic bacteria Pseudomonas syringae, but not against the necrotrophic fungus Botrytis cinerea. These findings are consistent with a role of cAMP-dependent pathways in the defense against biotrophic and hemibiotrophic plant pathogens.
AB - Adenylyl cyclases (ACs) catalyze the formation of the second messenger cAMP from ATP. Here we report the characterization of an Arabidopsis thaliana leucine-rich repeat (LRR) protein (At3g14460; AtLRRAC1) as an adenylyl cyclase. Using an AC-specific search motif supported by computational assessments of protein models we identify an AC catalytic center within the N-terminus and demonstrate that AtLRRAC1 can generate cAMP in vitro. Knock-out mutants of AtLRRAC1 have compromised immune responses to the biotrophic fungus Golovinomyces orontii and the hemibiotrophic bacteria Pseudomonas syringae, but not against the necrotrophic fungus Botrytis cinerea. These findings are consistent with a role of cAMP-dependent pathways in the defense against biotrophic and hemibiotrophic plant pathogens.
UR - http://hdl.handle.net/10754/629936
UR - https://www.sciencedirect.com/science/article/pii/S0176161718305650
UR - http://www.scopus.com/inward/record.url?scp=85057745002&partnerID=8YFLogxK
U2 - 10.1016/j.jplph.2018.10.025
DO - 10.1016/j.jplph.2018.10.025
M3 - Article
C2 - 30530199
SN - 0176-1617
VL - 232
SP - 12
EP - 22
JO - Journal of Plant Physiology
JF - Journal of Plant Physiology
ER -