Peculiar protein-protein interactions of the novel endoplasmic reticulum membrane protein Rcr1 and ubiquitin ligase Rsp5

Biosci Biotechnol Biochem. 2007 Jan;71(1):249-52. doi: 10.1271/bbb.60446. Epub 2007 Jan 7.

Abstract

Overproduction of the ER membrane protein Rcr1 makes Saccharomyces cerevisiae resistant to Congo red by reducing the chitin content through a unknown mechanism. By both co-immunoprecipitation and yeast two-hybrid experiments, specific interaction between Rcr1 and the ubiquitin ligase Rsp5 was found. This binding was largely mediated by a singular VPEY sequence in Rcr1 in addition to PPSY, the consensus ligand motif of the WW domains. Mutant analysis indicated that Rsp5 and other Rcr1-interacting proteins discovered in the current screen were not engaged in Congo red resistance.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Endoplasmic Reticulum / metabolism*
  • Endosomal Sorting Complexes Required for Transport
  • Membrane Proteins / genetics
  • Membrane Proteins / metabolism*
  • Protein Binding
  • Saccharomyces cerevisiae / genetics
  • Saccharomyces cerevisiae / metabolism
  • Saccharomyces cerevisiae Proteins / genetics
  • Saccharomyces cerevisiae Proteins / metabolism*
  • Ubiquitin-Protein Ligase Complexes / genetics
  • Ubiquitin-Protein Ligase Complexes / metabolism*

Substances

  • Endosomal Sorting Complexes Required for Transport
  • Membrane Proteins
  • Rcr1 protein, S cerevisiae
  • Saccharomyces cerevisiae Proteins
  • Ubiquitin-Protein Ligase Complexes
  • RSP5 protein, S cerevisiae