Regulatory interaction of PRL1 WD protein with Arabidopsis SNF1-like protein kinases.

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.
Mesh Terms:
Amino Acid Sequence, Arabidopsis, Arabidopsis Proteins, Carrier Proteins, Gene Expression Regulation, Plant, Genes, Fungal, Genes, Plant, Intracellular Signaling Peptides and Proteins, Molecular Sequence Data, Mutation, Nuclear Proteins, Plant Proteins, Protein Binding, Protein-Serine-Threonine Kinases, Sequence Alignment
Proc. Natl. Acad. Sci. U.S.A.
Date: Apr. 27, 1999
Download Curated Data For This Publication
48217
Switch View:
  • Interactions 8