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Functional differences in yeast protein disulfide isomerases.

P Nørgaard¹, V Westphal, C Tachibana

¹Department of Yeast Genetics, Carlsberg Laboratory, DK-2500 Copenhagen Valby, Denmark.

The Journal of Cell Biology

|February 7, 2001

Summary

Yeast protein disulfide isomerase (PDI) homologues are not interchangeable. Only Mpd1p fully restored function in PDI1-deleted yeast, highlighting the essential role of PDI in cellular processes.

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Area of Science:

Cellular Biology
Molecular Biology
Yeast Genetics

Background:

Protein disulfide isomerase (PDI) is crucial for protein folding in the endoplasmic reticulum.
Yeast Saccharomyces cerevisiae possesses one essential PDI gene (PDI1) and four homologous nonessential genes (MPD1, MPD2, EUG1, EPS1).

Purpose of the Study:

To investigate the functional redundancy and interchangeability of PDI homologues in yeast.
To determine the specific roles of MPD1, MPD2, EUG1, and EPS1 in relation to the essential PDI1 gene.

Main Methods:

Generating simultaneous deletion mutants of nonessential PDI homologues.
Assessing the ability of PDI homologues to restore viability to a pdi1-deleted strain via overexpression.
Analyzing the requirement of specific active site motifs (CXXC) for functional complementation.

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Main Results:

Homologue function is not interchangeable; restoration of viability in pdi1-deleted strains depends on endogenous levels of other homologues.
Mpd1p is the sole homologue capable of performing all essential functions of Pdi1p.
Functional complementation by EUG1 requires endogenous homologues with a CXXC motif, emphasizing the importance of oxidation activity.

Conclusions:

The PDI homologues exhibit specialized roles rather than complete functional redundancy.
Protein disulfide isomerase-catalyzed oxidation is essential, as indicated by the requirement for CXXC motifs.
Mutations affect carboxypeptidase Y folding and glycan modification but not ER-associated protein degradation.