Open AccessNovel receptor‐like kinases in cacao contain PR ‐1 extracellular domains
Author(s) -
Teixeira Paulo José Pereira Lima,
Costa Gustavo Gilson Lacerda,
Fiorin Gabriel Lorencini,
Pereira Gonçalo Amarante Guimarães,
Mondego Jorge Maurício Costa
Publication year - 2013
Publication title -
molecular plant pathology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.945
H-Index - 103
eISSN - 1364-3703
pISSN - 1464-6722
DOI - 10.1111/mpp.12028
Subject(s) - biology , protein kinase domain , kinase , transmembrane protein , transmembrane domain , genetics , gene , protein serine threonine kinases , phylogenetic tree , receptor , microbiology and biotechnology , protein kinase a , mutant
Summary Members of the pathogenesis‐related protein 1 ( PR ‐1) family are well‐known markers of plant defence responses, forming part of the arsenal of the secreted proteins produced on pathogen recognition. Here, we report the identification of two cacao ( T heobroma cacao L .) PR ‐1s that are fused to transmembrane regions and serine/threonine kinase domains, in a manner characteristic of receptor‐like kinases ( RLKs ). These proteins ( TcPR ‐1f and TcPR ‐1g) were named PR ‐1 receptor kinases ( PR ‐1 RK s). Phylogenetic analysis of RLKs and PR ‐1 proteins from cacao indicated that PR ‐1 RK s originated from a fusion between sequences encoding PR ‐1 and the kinase domain of a L ec RLK ( L ectin R eceptor‐ L ike K inase). Retrotransposition marks surround TcPR ‐1f , suggesting that retrotransposition was involved in the origin of PR ‐1 RK s. Genes with a similar domain architecture to cacao PR ‐1 RK s were found in rice ( O ryza sativa ), barrel medic ( M edicago truncatula ) and a nonphototrophic bacterium ( H erpetosiphon aurantiacus ). However, their kinase domains differed from those found in L ec RLK s, indicating the occurrence of convergent evolution. TcPR ‐1g expression was up‐regulated in the biotrophic stage of witches' broom disease, suggesting a role for PR ‐1 RK s during cacao defence responses. We hypothesize that PR ‐1 RK s transduce a defence signal by interacting with a PR ‐1 ligand.