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Biochim. Biophys. Acta Feb (2007); 1773(2):232-42
The Saccharomyces cerevisiae YFR041C-ERJ5 gene encoding a type I membrane protein with a J domain is required to preserve the folding capacity of the endoplasmic reticulum-
Carla Fama M, Raden D, Zacchi N, Lemos DR, Robinson AS, Silberstein S
IBYF-CONICET, Catedra de Microbiologia, Facultad de Agronomia, Universidad de Buenos Aires, Avda- San Martin 4453, C1417DSE Buenos Aires, Argentina-
Abstract: YFR041C-ERJ5 was identified in Saccharomyces cerevisiae as a gene regulated by the unfolded protein response pathway -UPR-- The open reading frame of the gene has a J domain characteristic of the DnaJ chaperone family of proteins that regulate the activity of Hsp70 chaperones- We determined the expression and topology of Erj5p, a type I membrane protein with a J domain in the lumen of the endoplasmic reticulum -ER- that colocalizes with Kar2p, the major Hsp70 in the yeast ER- We identified synthetic interactions of Deltaerj5 with mutations in genes involved in protein folding in the ER -kar2-159, Deltascj1Deltajem1- and in the induction of the unfolded protein response -Deltaire1-- Loss of Erj5p in yeast cells with impaired ER protein folding capacity increased sensitivity to agents that cause ER stress- We identified the ERJ5 mRNA and confirmed that agents that promote accumulation of misfolded proteins in the ER regulate its abundance- We found that loss of the non-essential ERJ5 gene leads to a constitutively induced UPR, indicating that ERJ5 is required for maintenance of an optimal folding environment in the yeast ER-
[PUBMED: 17157937] Download Biogrid Interactions in a variety of formats including PSI FormatPUBMED
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Chris Stark, Bobby-Joe Breitkreutz, Teresa Reguly, Lorrie Boucher, Ashton Breitkreutz, Mike Tyers.
Nucleic Acids Res. Jan 1;34:D535-9.