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Hut1 proteins identified in Saccharomyces cerevisiae and Schizosaccharomyces pombe are functional homologues involved in the protein‐folding process at the endoplasmic reticulum
Author(s) -
Nakanishi Hideki,
Nakayama Kenichi,
Yokota Ayako,
Tachikawa Hiroyuki,
Takahashi Nobuhiro,
Jigami Yoshifumi
Publication year - 2001
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.707
Subject(s) - schizosaccharomyces pombe , endoplasmic reticulum , biology , saccharomyces cerevisiae , folding (dsp implementation) , protein folding , microbiology and biotechnology , schizosaccharomyces , computational biology , yeast , biochemistry , genetics , engineering , electrical engineering
The Saccharomyces cerevisiae HUT1 gene (sc HUT1 ) and the Schizosaccharomyces pombe hut1 + gene (sp hut1 + ) encode hydrophobic proteins with approximately 30% identity to a human UDP–galactose transporter‐related gene ( UGTrel1 ) product. These proteins show a significant similarity to the nucleotide sugar transporter and are conserved in many eukaryotic species, but their physiological functions are not known. Both sc HUT1 and sp hut1 + genes are non‐essential for cell growth under normal conditions, and their disruptants show no defects in the modification of O ‐ and N ‐linked oligosaccharides, but are sensitive to a membrane‐permeable reducing agent, dithiothreitol (DTT). Consistent with this phenotype, sc HUT1 has genetic interaction with ERO1 , which plays an essential role in the oxidation of secretory proteins at the endoplasmic reticulum (ER). Overexpression of the MPD1 or MPD2 genes, which were isolated as multicopy suppressors of protein disulphide isomerase (PDI) depletion, could not replace the essential function of PDI in Δhut1 S. cerevisiae cells. Our results indicate that scHut1p and spHut1p are functional homologues, and their physiological function is to maintain the optimal environment for the folding of secretory pathway proteins in the ER. Copyright © 2001 John Wiley & Sons, Ltd.