ArticleBiochimica et biophysica acta2007
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.
Article in Biochimica et biophysica acta, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 37 citations in OpenAlex.
- Differential roles of Scj1 and Djp1, two DnaJ homologs, in virulence, cell wall integrity, and multi-stress tolerance of Beauveria bassiana.Antonie van Leeuwenhoek · 2026Article
- Article
- Translational Regulation of Pmt1 and Pmt2 by Bfr1 Affects Unfolded Protein O-Mannosylation.International journal of molecular sciences · 2019Article
- A novel fusion partner for enhanced secretion of recombinant proteins in Saccharomyces cerevisiae.Applied microbiology and biotechnology · 2016Article
- The interplay of Hrd3 and the molecular chaperone system ensures efficient degradation of malfolded secretory proteins.Molecular biology of the cell · 2015Article
- The proteome and phosphoproteome of Neurospora crassa in response to cellulose, sucrose and carbon starvation.Fungal genetics and biology : FG & B · 2014Article
- Emerging features of ER resident J-proteins in plants.Plant signaling & behavior · 2014Review
- Different expression systems for production of recombinant proteins in Saccharomyces cerevisiae.Biotechnology and bioengineering · 2012Article
- Imbalance of heterologous protein folding and disulfide bond formation rates yields runaway oxidative stress.BMC biology · 2012Article
- Arabidopsis thaliana J-class heat shock proteins: cellular stress sensors.Functional & integrative genomics · 2009Review
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Authors and funding
6 authors at 2 institutions in 2 countries.
Funding
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.
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