Peculiar protein-protein interactions of the novel endoplasmic reticulum membrane protein Rcr1 and ubiquitin ligase Rsp5.
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.
Imai
Keita
K
Department of Biotechnology, University of Tokyo, Japan.
Noda
Yoichi
Y
Adachi
Hiroyuki
H
Yoda
Koji
K
D004721:Endoplasmic Reticulum / Q000378:metabolism*; D056827:Endosomal Sorting Complexes Required for Transport; D008565:Membrane Proteins / Q000235:genetics / Q000378:metabolism*; D011485:Protein Binding; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000235:genetics / Q000378:metabolism*; D043743:Ubiquitin-Protein Ligase Complexes / Q000235:genetics / Q000378:metabolism*
D056827:Endosomal Sorting Complexes Required for Transport; D008565:Membrane Proteins; C498876:Rcr1 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; D043743:Ubiquitin-Protein Ligase Complexes; C469287:RSP5 protein, S cerevisiae