Inositol polyphosphate kinase activity of Arg82/ArgRIII is not required for the regulation of the arginine metabolism in yeast

FEBS Lett. 2000 Dec 15;486(3):300-4. doi: 10.1016/s0014-5793(00)02318-8.

Abstract

Arg82, a nuclear regulator of diverse cellular processes in yeast, is an inositol polyphosphate kinase. Some defects such as the regulation of arginine metabolism observed in an arg82Delta, result from a lack of Mcm1 and Arg80 stability. We show here that neither the kinase activity of Arg82 nor inositol phosphates are required for the control of arginine metabolism. Arg82 mutations keeping kinase active affect the expression of arginine genes, whereas mutations in the kinase domain do not impair this metabolic control.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Arginine / metabolism*
  • Binding Sites / genetics
  • Cell Division / genetics
  • Fungal Proteins / genetics
  • Fungal Proteins / metabolism*
  • Gene Deletion
  • Inositol Phosphates / metabolism*
  • Mutagenesis, Site-Directed
  • Phosphotransferases (Alcohol Group Acceptor) / metabolism
  • Point Mutation
  • Saccharomyces cerevisiae / metabolism*
  • Saccharomyces cerevisiae Proteins*
  • Type C Phospholipases / deficiency
  • Type C Phospholipases / genetics
  • Type C Phospholipases / metabolism

Substances

  • Fungal Proteins
  • Inositol Phosphates
  • Saccharomyces cerevisiae Proteins
  • Arginine
  • ARG82 protein, S cerevisiae
  • Phosphotransferases (Alcohol Group Acceptor)
  • Inositol 1,4,5-trisphosphate 3-kinase
  • Type C Phospholipases