Arabidopsis extra large G-protein 2 (XLG2) interacts with the Gβ subunit of heterotrimeric G protein and functions in disease resistance

Huifen Zhu, Guo Jing Li, Lei Ding, Xiangqin Cui, Howard Berg, Sarah M. Assmann, Yiji Xia

Research output: Contribution to journalArticlepeer-review

68 Scopus citations

Abstract

Heterotrimeric GTP-binding proteins, which consist of Gα, Gβ, and Gγ subunits, play important roles in transducing extracellular signals perceived by cell surface receptors into intracellular physiological responses. In addition to a single prototypical Ga protein (GPA1), Arabidopsis has three unique Ga-like proteins, known as XLG1, XLG2, and XLG3, that have been found to be localized in nuclei, although their functions and mode of action remain largely unknown. Through a transcriptomic analysis, we found that XLG2 and XLG3 were rapidly induced by infection with the bacterial pathogen Pseudomonas syringae, whereas the XLG1 transcript level was not affected by pathogen infection. A reverse genetic screen revealed that the xlg2 loss-of-function mutation causes enhanced susceptibility to P. syringae. Transcriptome profiling revealed that the xlg2 mutation affects pathogen-triggered induction of a small set of defense-related genes. However, xlg1 and xlg3 mutants showed no difference from wild-type plants in resistance to P. syringae. In addition, the xlg2 xlg3 double mutant and the xlg1 xlg2 xlg3 triple mutant were not significantly different from the xlg2 single mutant in the disease resistance phenotype, suggesting that the roles of XLG1 and XLG3 in defense, if any, are less significant than for XLG2. Constitutive overexpression of XLG2 leads to the accumulation of abnormal transcripts from multiple defense-related genes. Through co-immunoprecipitation assays, XLG2 was found to interact with AGB1, the sole Gb subunit in Arabidopsis, which has previously been found to be a positive regulator in resistance to necrotrophic fungal pathogens. However, no significant difference was found between three xlg single mutants, the xlg2 xlg3 double mutant, the xlg triple mutant, and wild-type plants in resistance to the necrotrophic fungal pathogens Botrytis cinerea or Alternaria brassicicola. These results suggest that XLG2 and AGB1 are components of a G-protein complex different from the prototypical heterotrimeric G-protein and may have distinct functions in modulating defense responses.

Original languageEnglish (US)
Pages (from-to)513-525
Number of pages13
JournalMolecular plant
Volume2
Issue number3
DOIs
StatePublished - May 2009

All Science Journal Classification (ASJC) codes

  • Molecular Biology
  • Plant Science

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