Reference - PMID:15449306 - Schizosaccharomyces pombe ER oxidoreductin-like proteins SpEro1a p and SpEro1b p.
Reference summary
- PubMed ID
- PMID:15449306
- Title
- Schizosaccharomyces pombe ER oxidoreductin-like proteins SpEro1a p and SpEro1b p.
- Authors
- Kettner K, Blomberg A, Rödel G
- Citation
- Yeast 2004 Sep;21(12):1035-44
- Publication year
- 2004
- Abstract
- Endoplasmic reticulum oxidoreductins (Ero proteins) are essential for oxidation of protein disulphide isomerase (Pdi), which introduces disulphide bonds in target proteins. Contrary to the situation in Saccharomyces cerevisiae, with a single Ero protein (Ero1p), the genomes of Schizosaccharomyces pombe and of humans encode two Ero-like proteins. Here we show that both Sz. pombe proteins (SpEro1a p and SpEro1b p) are N-glycosylated and firmly associated with membranes of the secretory pathway. Surprisingly, only expression of SpEro1b p completely restores growth of the temperature-sensitive S. cerevisiae ero1-1 mutant, whereas SpEro1a p only partially complements this mutation. Upon expression in S. cerevisiae wild-type cells, SpEro1b p leads to a significantly increased resistance to reductive stress by dithiothreitol, whereas SpEro1a p has only a marginal effect. These data suggest that SpEro1b p is a functional homologue of the S. cerevisiae Ero1p.
