Abstract

Plant cell walls are embedded in a pectin matrix which is physically linked with the wall-associated kinases (WAKs), a subfamily of receptor-like kinases that participate in the cell wall integrity (CWI) sensing. Since cell walls are also the main binding sites for boron (B) and aluminum (Al), WAK may be potentially associated with the regulation of plant responses to Al toxicity and B deficiency. Using pea as a model species, we have identified a total of 28 WAK genes in the genome and named them according to its chromosomal location. All the PsWAKs were phylogenetically grouped into three clades. Phylogenetic relationship and synteny analysis showed that the PsWAKs in pea and Glycine max or Medicago truncatula shared a relatively conserved evolutionary history. Protein domain, motif, and transmembrane analysis indicated that all PsWAK proteins were predicted to be localized to the plasma membrane, and most PsWAKs shared a similar structure to their homologs. The RNA-seq data showed that the expression pattern of WAK genes in response to B deficiency was similar to that of Al toxicity, with most of PsWAKs being up-regulated. The qRT-PCR results further confirmed that PsWAK5, PsWAK9 and PsWAK14 were more specific for both B-deficiency and Al toxicity, and the expression levels of PsWAK5, PsWAK9 and PsWAK14 were significantly higher in the Al-sensitive cultivar Hyogo than in the Al-resistant cultivar Alaska under Al toxicity. This study provided an important basis for the functional and evolutionary analysis of PsWAKs and linked them to responses to cell wall damage induced by B-deficiency and Al toxicity, suggesting that PsWAKs may play a key role in the perception of cell wall integrity under Al toxicity or B-deficiency, as well as in the regulation of Al tolerance in pea.

Full Text
Paper version not known

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call

Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.