Schizosaccharomyces pombe ER oxidoreductin-like proteins SpEro1a p and SpEro1b p
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Updated: Aug 21, 2026

Genetic Screen for Identification of Multicopy Suppressors in Schizosaccharomyces pombe
Published on: September 13, 2022
Karina Kettner1, Anders Blomberg, Gerhard Rödel
1Institute for Genetics, Dresden University of Technology, D-01262, Germany.
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.
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