title: Regulatory interaction of PRL1 WD protein with Arabidopsis SNF1-like protein kinases.
abstract: Mutation of the PRL1 gene, encoding a regulatory WD protein, results in glucose hypersensitivity and derepression of glucose-regulated genes in Arabidopsis. The yeast SNF1 protein kinase, a key regulator of glucose signaling, and Arabidopsis SNF1 homologs AKIN10 and AKIN11, which can complement the Deltasnf1 mutation, were found to interact with an N-terminal domain of the PRL1 protein in the two-hybrid system and in vitro. AKIN10 and AKIN11 suppress the yeast Deltasnf4 mutation and interact with the SNF4p-activating subunit of SNF1. PRL1 and SNF4 bind independently to adjacent C-terminal domains of AKIN10 and AKIN11, and these protein interactions are negatively regulated by glucose in yeast. AKIN10 and AKIN11, purified in fusion with glutathione S-transferase, undergo autophosphorylation and phosphorylate a peptide of sucrose phosphate synthase in vitro. The sucrose phosphate synthase-peptide kinase activity of AKIN complexes detected by immunoprecipitation is stimulated by sucrose in light-grown Arabidopsis plants. In comparison with wild type, the activation level of AKIN immunocomplexes is higher in the prl1 mutant, suggesting that PRL1 is a negative regulator of Arabidopsis SNF1 homologs. This conclusion is supported by the observation that PRL1 is an inhibitor of AKIN10 and AKIN11 in vitro.
authors.affiliation: Max-Planck Institut für Züchtungsforschung, D-50829 Cologne, Germany.
authors.forename: R P
authors.initials: RP
authors.lastname: Bhalerao
authors.forename: K
authors.initials: K
authors.lastname: Salchert
authors.forename: L
authors.initials: L
authors.lastname: Bakó
authors.forename: L
authors.initials: L
authors.lastname: Okrész
authors.forename: L
authors.initials: L
authors.lastname: Szabados
authors.forename: T
authors.initials: T
authors.lastname: Muranaka
authors.forename: Y
authors.initials: Y
authors.lastname: Machida
authors.forename: J
authors.initials: J
authors.lastname: Schell
authors.forename: C
authors.initials: C
authors.lastname: Koncz
mesh_terms: D000595:Amino Acid Sequence; D017360:Arabidopsis / Q000235:genetics* / Q000378:metabolism; D029681:Arabidopsis Proteins; D002352:Carrier Proteins / Q000235:genetics* / Q000378:metabolism; D018506:Gene Expression Regulation, Plant; D005800:Genes, Fungal; D017343:Genes, Plant; D047908:Intracellular Signaling Peptides and Proteins; D008969:Molecular Sequence Data; D009154:Mutation; D009687:Nuclear Proteins / Q000235:genetics* / Q000378:metabolism; D010940:Plant Proteins / Q000235:genetics* / Q000378:metabolism; D011485:Protein Binding; D017346:Protein Serine-Threonine Kinases / Q000235:genetics* / Q000378:metabolism; D016415:Sequence Alignment
chemical_list: D029681:Arabidopsis Proteins; D002352:Carrier Proteins; D047908:Intracellular Signaling Peptides and Proteins; D009687:Nuclear Proteins; C492005:PRL1 protein, Arabidopsis; C115165:PRL1 protein, plant; D010940:Plant Proteins; C071570:SNF1-related protein kinases; D017346:Protein Serine-Threonine Kinases