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

被引:53
作者
Bianchet, Chantal [1 ]
Wong, Aloysius [2 ]
Quaglia, Mara [3 ]
Alqurashi, May [4 ]
Gehring, Chris [1 ,4 ]
Ntoukakis, Vardis [5 ,6 ]
Pasqualini, Stefania [1 ]
机构
[1] Univ Perugia, Dept Chem Biol & Biotechnol, Borgo 20 Giugno 74, I-06121 Perugia, Italy
[2] Wenzhou Kean Univ, Coll Sci & Technol, 88 Daxue Rd, Wenzhou 325060, Zhejiang, Peoples R China
[3] Univ Perugia, Dept Agr Food & Environm Sci, Borgo 20 Giugno 74, I-06121 Perugia, Italy
[4] 4700 King Abdullah Univ Sci & Technol, Biol & Environm Sci & Engn Div, Thuwal 239556900, Saudi Arabia
[5] Univ Warwick, Sch Life Sci, Coventry CV4 7AL, W Midlands, England
[6] Univ Warwick, Warwick Integrat Synthet Biol Ctr, Coventry CV4 7AL, W Midlands, England
基金
中国国家自然科学基金; 英国生物技术与生命科学研究理事会;
关键词
cAMP; Adenylyl cyclase; Arabidopsis thaliana; Botrytis cinerea; Golovinomyces orontii; Pseudomonas syringae pv. tomato; NBS-LRR PROTEINS; GUANYLYL CYCLASE; DISEASE-RESISTANCE; CYCLIC-AMP; GENE; CAMP; RECEPTOR; DEFENSE; CALCIUM; CA2+;
D O I
10.1016/j.jplph.2018.10.025
中图分类号
Q94 [植物学];
学科分类号
071001 ;
摘要
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.
引用
收藏
页码:12 / 22
页数:11
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