Classification and phylogenetic analyses of the Arabidopsis and tomato G-type lectin receptor kinases

Abstract

BackgroundPathogen perception by plants is mediated by plasma membrane-localized immune receptors that have varied extracellular domains. Lectin receptor kinases (LecRKs) are among these receptors and are subdivided into 3 classes, C-type LecRKs (C-LecRKs), L-type LecRKs (L-LecRKs) and G-type LecRKs (G-LecRKs). While C-LecRKs are represented by one or two members in all plant species investigated and have unknown functions, L-LecRKs have been characterized in a few plant species and have been shown to play roles in plant defense against pathogens. Whereas Arabidopsis G-LecRKs have been characterized, this family of LecRKs has not been studied in tomato.ResultsThis investigation updates the current characterization of Arabidopsis G-LecRKs and characterizes the tomato G-LecRKs, using LecRKs from the monocot rice and the basal eudicot columbine to establish a basis for comparisons between the two core eudicots. Additionally, revisiting parameters established for Arabidopsis nomenclature for LecRKs is suggested for both Arabidopsis and tomato. Moreover, using phylogenetic analysis, we show the relationship among and between members of G-LecRKs from all three eudicot plant species. Furthermore, investigating presence of motifs in G-LecRKs we identified conserved motifs among members of G-LecRKs in tomato and Arabidopsis, with five present in at least 30 of the 38 Arabidopsis members and in at least 45 of the 73 tomato members.ConclusionsThis work characterized tomato G-LecRKs and added members to the currently characterized Arabidopsis G-LecRKs. Additionally, protein sequence analysis showed an expansion of this family in tomato as compared to Arabidopsis, and the existence of conserved common motifs in the two plant species as well as conserved species-specific motifs.Electronic supplementary materialThe online version of this article (10.1186/s12864-018-4606-0) contains supplementary material, which is available to authorized users.

De novo Assembly of Transcriptomes From a B73 Maize Line Introgressed With a QTL for Resistance to Gray Leaf Spot Disease Reveals a Candidate Allele of a Lectin Receptor-Like Kinase

“…Domain analysis of L-RLK-CML showed that it contained all the functional domains of a G-type lectin receptor-like kinase (extracellular mannose-binding lectin, S-locus glycoprotein, and PAN-like domains, a trans-membrane domain, and the intracellular kinase domain). G-type receptor-like kinases (previously categorized as Bulb-or B-type due to their frequent occurrence in bulb species) are one of three classes of lectin receptor-like kinases (Teixeira et al, 2018). The bestcharacterized representatives of G-type L-RLKs are those that function in self-incompatibility, which is a mechanism that deters inbreeding in angiosperms (Kusaba et al, 2001).…”

“…There are an estimated 38 G-type L-RLK SD1 genes in Arabidopsis (Teixeira et al, 2018), and therefore they do not only play a role in self-incompatibility. They are involved in a range of developmental and environmental stress responses, including response to biotic stress (Vaid et al, 2013).…”

Genes for ash tree resistance to an insect pest identified via comparative genomics

“…with some having a role in plant defence 111,112 such as in response to the tobacco hawk moth (Manduca sexta) in Nicotiana attenuata 113 or to the brown planthopper (Nilaparvata lugens) in rice 114 . Extracellular ATP is associated with cell damage, and perception of ATP may play a role in defence response against insect herbivores via stimulation of the JA pathway 27 .…”

“…Extracellular ATP is associated with cell damage, and perception of ATP may play a role in defence response against insect herbivores via stimulation of the JA pathway 27 . AT5G24080 has also been named AtG-LecRK-I.6 by Teixeira et al 111 , who suggest it may be defective because its protein has an incomplete kinase domain and lacks some of the subdomains typically found in kinases. However, such proteins may still be functional even if they lack kinase activity 111 Table 5).…”

“…AT5G24080 has also been named AtG-LecRK-I.6 by Teixeira et al 111 , who suggest it may be defective because its protein has an incomplete kinase domain and lacks some of the subdomains typically found in kinases. However, such proteins may still be functional even if they lack kinase activity 111 Table 5).…”