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Schizosaccharomyces pombe ER oxidoreductin‐like proteins SpEro1a p and SpEro1b p
Author(s) -
Kettner Karina,
Blomberg Anders,
Rödel Gerhard
Publication year - 2004
Publication title -
yeast
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.923
H-Index - 102
eISSN - 1097-0061
pISSN - 0749-503X
DOI - 10.1002/yea.1149
Subject(s) - schizosaccharomyces pombe , saccharomyces cerevisiae , dithiothreitol , endoplasmic reticulum , biology , mutant , schizosaccharomyces , yeast , wild type , biochemistry , mutation , microbiology and biotechnology , gene , enzyme
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. Copyright © 2004 John Wiley & Sons, Ltd.