Department of Chemistry, Biology and Biotechnology, University of Perugia, Borgo XX giugno, 74, 06121 Perugia, Italy.
College of Science and Technology, Wenzhou-Kean University, 88 Daxue Road, Ouhai, Wenzhou, Zhejiang Province, 325060, China.
J Plant Physiol. 2019 Jan;232:12-22. doi: 10.1016/j.jplph.2018.10.025. Epub 2018 Nov 3.
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.
腺苷酸环化酶（ACs）催化 ATP 生成第二信使 cAMP。在这里，我们报告了拟南芥亮氨酸丰富重复（LRR）蛋白（At3g14460；AtLRRAC1）作为腺苷酸环化酶的特性。使用由蛋白质模型的计算评估支持的 AC 特异性搜索基序，我们在 N 端鉴定出 AC 催化中心，并证明 AtLRRAC1 可以在体外生成 cAMP。AtLRRAC1 的敲除突变体对生物营养真菌 Golovinomyces orontii 和半生物营养细菌 Pseudomonas syringae 的免疫反应受损，但对坏死真菌 Botrytis cinerea 没有受损。这些发现与 cAMP 依赖性途径在防御生物营养和半生物营养植物病原体中的作用一致。
