A point mutation in the kinase domain of CRK10 leads to xylem vessel collapse and activation of defence responses in Arabidopsis

© The Author(s) 2023. Published by Oxford University Press on behalf of the Society for Experimental Biology.

Bibliographische Detailangaben
Veröffentlicht in:Journal of experimental botany. - 1985. - 74(2023), 10 vom: 19. Mai, Seite 3104-3121
1. Verfasser: Piovesana, Maiara (VerfasserIn)
Weitere Verfasser: Wood, Ana K M, Smith, Daniel P, Deery, Michael J, Bayliss, Richard, Carrera, Esther, Wellner, Nikolaus, Kosik, Ondrej, Napier, Johnathan A, Kurup, Smita, Matthes, Michaela C
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2023
Zugriff auf das übergeordnete Werk:Journal of experimental botany
Schlagworte:Journal Article Research Support, Non-U.S. Gov't Fusarium oxysporum Arabidopsis cysteine-rich receptor-like kinase CRK10 defence response gain-of-function mutation kinase regulation transcriptomics xylem vessel collapse mehr... αC helix Arabidopsis Proteins Protein Kinases EC 2.7.- Protein Serine-Threonine Kinases EC 2.7.11.1
Beschreibung
Zusammenfassung:© The Author(s) 2023. Published by Oxford University Press on behalf of the Society for Experimental Biology.
Cysteine-rich receptor-like kinases (CRKs) are a large family of plasma membrane-bound receptors ubiquitous in higher plants. However, despite their prominence, their biological roles have remained largely elusive so far. In this study we report the characterization of an Arabidopsis mutant named crk10-A397T in which alanine 397 has been replaced by a threonine in the αC helix of the kinase domain of CRK10, known to be a crucial regulatory module in mammalian kinases. The crk10-A397T mutant is a dwarf that displays collapsed xylem vessels in the root and hypocotyl, whereas the vasculature of the inflorescence develops normally. In situ phosphorylation assays with His-tagged wild type and crk10-A397T versions of the CRK10 kinase domain revealed that both alleles are active kinases capable of autophosphorylation, with the newly introduced threonine acting as an additional phosphorylation site in crk10-A397T. Transcriptomic analysis of wild type and crk10-A397T mutant hypocotyls revealed that biotic and abiotic stress-responsive genes are constitutively up-regulated in the mutant, and a root-infection assay with the vascular pathogen Fusarium oxysporum demonstrated that the mutant has enhanced resistance to this pathogen compared with wild type plants. Taken together our results suggest that crk10-A397T is a gain-of-function allele of CRK10, the first such mutant to have been identified for a CRK in Arabidopsis
Beschreibung:Date Completed 12.06.2023
Date Revised 12.06.2023
published: Print
Citation Status MEDLINE
ISSN:1460-2431
DOI:10.1093/jxb/erad080