Mutation of a putative AMPK phosphorylation site abolishes the repressor activity but not the nuclear targeting of the fungal glucose regulator CRE1

Curr Genet. 2000 May;37(5):328-32. doi: 10.1007/s002940050535.

Abstract

In filamentous ascomycetes, glucose repression is mediated by CRE1, a zinc-finger protein related to Miglp from yeast. Five putative AMPK phosphorylation motifs identified in the glucose repressor from the phytopathogenic fungus Sclerotinia sclerotiorum were mutated in a GFP::CRE1 translational fusion. Complementation experiments in Aspergillus nidulans and fluorescence microscopy analyses showed that mutation of one site (Ser266) abolishes the repressor activity of the fusion protein but not its nuclear targeting, suggesting that an AMPK protein kinase may be involved in the function of the fungal glucose repressor.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • AMP-Activated Protein Kinases
  • Amino Acid Motifs
  • Cell Nucleus / metabolism
  • DNA-Binding Proteins / genetics*
  • DNA-Binding Proteins / metabolism*
  • Fungal Proteins*
  • Glucose / metabolism*
  • Green Fluorescent Proteins
  • Luminescent Proteins / genetics
  • Luminescent Proteins / metabolism
  • Microscopy, Fluorescence
  • Multienzyme Complexes / metabolism*
  • Mutagenesis, Site-Directed
  • Mutation*
  • Phosphorylation
  • Protein Serine-Threonine Kinases / metabolism*
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / metabolism
  • Repressor Proteins / genetics*
  • Repressor Proteins / metabolism*
  • Serine

Substances

  • DNA-Binding Proteins
  • Fungal Proteins
  • Luminescent Proteins
  • Multienzyme Complexes
  • Recombinant Fusion Proteins
  • Repressor Proteins
  • Green Fluorescent Proteins
  • Serine
  • Protein Serine-Threonine Kinases
  • AMP-Activated Protein Kinases
  • Glucose