Abstract
Glycine max has 32 mitogen activated protein kinases (MAPKs), nine of them exhibiting defense functions (defense MAPKs) to the plant parasitic nematode Heterodera glycines. RNA seq analyses of transgenic G. max lines overexpressing (OE) each defense MAPK has led to the identification of 309 genes that are increased in their relative transcript abundance by all 9 defense MAPKs. Here, 71 of those genes are shown to also have measurable amounts of transcript in H. glycines-induced nurse cells (syncytia) produced in the root that are undergoing a defense response. The 71 genes have been grouped into 7 types, based on their expression profile. Among the 71 genes are 8 putatively-secreted proteins that include a galactose mutarotase-like protein, pollen Ole e 1 allergen and extensin protein, endomembrane protein 70 protein, O-glycosyl hydrolase 17 protein, glycosyl hydrolase 32 protein, FASCICLIN-like arabinogalactan protein 17 precursor, secreted peroxidase and a pathogenesis-related thaumatin protein. Functional transgenic analyses of all 8 of these candidate defense genes that employ their overexpression and RNA interference (RNAi) demonstrate they have a role in defense. Overexpression experiments that increase the relative transcript abundance of the candidate defense gene reduces the ability that the plant parasitic nematode Heterodera glycines has in completing its life cycle while, in contrast, RNAi of these genes leads to an increase in parasitism. The results provide a genomic analysis of the importance of MAPK signaling in relation to the secretion apparatus during the defense process defense in the G. max-H. glycines pathosystem and identify additional targets for future studies.
Highlights
Plants, like many organisms, respond to a number of biotic and abiotic challenges
The annotation of the mitogen activated protein kinases (MAPKs) gene family presented by McNeece et al [11] had been based off of earlier studies that led to the identification of different numbers of MAPKs
McNeece et al [11] presented a specific set of criteria used to select the chosen G. max MAPKs, based off of comparisons made to MAPKs already identified in A. thaliana and those already identified in G. max
Summary
Like many organisms, respond to a number of biotic and abiotic challenges These responses occur through complex signal transduction processes. Input information is processed through a stepwise series of phosphorylation events whereby MAP kinase kinase kinases (MAPKKKs) phosphorylate MAP kinase kinases (MAPKKs) that in turn phosphorylate MAPKs [5]. These events lead to an appropriate output response [5]. Due to this stepwise, shared processing, it has been determined that the MAPK cascade works as a cooperative enzyme, switching cells from one discrete state to another [6]
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