title: Arabidopsis extra-large G proteins (XLGs) regulate root morphogenesis.
abstract: As in mammalian systems, heterotrimeric G proteins, composed of alpha, beta and gamma subunits, are present in plants and are involved in the regulation of development and cell signaling. Besides the sole prototypical G protein alpha subunit gene, GPA1, the Arabidopsis thaliana genome has three extra-large GTP-binding protein (XLG)-encoding genes: XLG1 (At2g23460), XLG2 (At4g34390) and XLG3 (At1g31930). The C-termini of the XLGs are Galpha domains that are homologous to GPA1, whereas their N-termini each contain a cysteine-rich region and a putative nuclear localization signal (NLS). GFP fusions with each XLG confirmed nuclear localization. All three XLG genes are expressed in essentially all plant organs, with strong expression in vascular tissues, primary root meristems and lateral root primordia. Analysis of single, double and triple T-DNA insertional mutants of the XLG genes revealed redundancy in XLG function. Dark-grown xlg1-1 xlg2-1 xlg3-1 triple mutant plants showed markedly increased primary root length compared with wild-type plants. This phenotype was not observed in dark-grown xlg single mutants, and was suppressed upon complementation of the xlg triple mutant with each XLG. Root cell sizes of the xlg triple mutant and root morphology were highly similar to those of wild-type roots, suggesting that XLGs may regulate cell proliferation. Dark-grown roots of the xlg triple mutants also showed altered sensitivity to sugars, ABA hyposensitivity and ethylene hypersensitivity, whereas seed germination in xlg triple mutants was hypersensitive to osmotic stress and ABA. As plant-specific proteins, regulatory mechanisms of XLGs may differ from those of conventional Galphas.
authors.affiliation: Biology Department, Penn State University, University Park, Pennsylvania 16802, USA.
authors.forename: Lei
authors.initials: L
authors.lastname: Ding
authors.forename: Sona
authors.initials: S
authors.lastname: Pandey
authors.forename: Sarah M
authors.initials: SM
authors.lastname: Assmann
mesh_terms: D000040:Abscisic Acid / Q000494:pharmacology; D000595:Amino Acid Sequence; D017360:Arabidopsis / Q000235:genetics / Q000254:growth & development / Q000502:physiology*; D029681:Arabidopsis Proteins / Q000737:chemistry / Q000235:genetics / Q000502:physiology*; D002241:Carbohydrates / Q000494:pharmacology; D002467:Cell Nucleus / Q000378:metabolism; D005030:Ethylenes / Q000494:pharmacology; D019204:GTP-Binding Proteins / Q000737:chemistry / Q000235:genetics / Q000502:physiology*; D018525:Germination / Q000187:drug effects; D020962:Heterotrimeric GTP-Binding Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D008969:Molecular Sequence Data; D009024:Morphogenesis; D009154:Mutation; D018517:Plant Roots / Q000254:growth & development* / Q000378:metabolism; D016415:Sequence Alignment
chemical_list: D029681:Arabidopsis Proteins; D002241:Carbohydrates; D005030:Ethylenes; C120055:XLG1 protein, Arabidopsis; D000040:Abscisic Acid; C036216:ethylene; D019204:GTP-Binding Proteins; D020962:Heterotrimeric GTP-Binding Proteins; C527829:XLG2 protein, Arabidopsis; C527830:XLG3 protein, Arabidopsis