An Arabidopsis thaliana leucine-rich repeat protein harbors an adenylyl cyclase catalytic center and affects responses to pathogens

Chantal Bianchet; Aloysius Tze Wong; Mara Quaglia; May Majed Alquraishi; Christoph A Gehring; Vardis Ntoukakis; Stefania Pasqualini

doi:10.1016/j.jplph.2018.10.025

An Arabidopsis thaliana leucine-rich repeat protein harbors an adenylyl cyclase catalytic center and affects responses to pathogens

Chantal Bianchet, Aloysius Tze Wong, Mara Quaglia, May Majed Alquraishi, Christoph A Gehring, Vardis Ntoukakis, Stefania Pasqualini

Research output: Contribution to journal › Article › peer-review

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Abstract

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.

Original language	English (US)
Pages (from-to)	12-22
Number of pages	11
Journal	Journal of Plant Physiology
Volume	232
DOIs	https://doi.org/10.1016/j.jplph.2018.10.025
State	Published - Nov 3 2018

Bibliographical note

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).

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https://repository.kaust.edu.sa/bitstream/10754/629936/1/1-s2.0-S0176161718305650-main.pdf

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title = "An Arabidopsis thaliana leucine-rich repeat protein harbors an adenylyl cyclase catalytic center and affects responses to pathogens",

abstract = "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.",

author = "Chantal Bianchet and Wong, {Aloysius Tze} and Mara Quaglia and Alquraishi, {May Majed} and Gehring, {Christoph A} and Vardis Ntoukakis and Stefania Pasqualini",

note = "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 Ale{\v s} Lebeda and Bo{\v z}ena Sedl{\'a}kov{\'a} (Palack{\'y} 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).",

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AU - Bianchet, Chantal

AU - Wong, Aloysius Tze

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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

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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.

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An Arabidopsis thaliana leucine-rich repeat protein harbors an adenylyl cyclase catalytic center and affects responses to pathogens

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