scholarly journals Nucleotide Sequence and Developmental Expression of Duplicated Genes Encoding Protein Disulfide Isomerase in Barley (Hordeum vulgare L.)

1994 ◽  
Vol 106 (4) ◽  
pp. 1705-1706 ◽  
Author(s):  
F. Chen ◽  
P. M. Hayes
Keyword(s):  
Hordeum Vulgare ◽  
Nucleotide Sequence ◽  
Protein Disulfide Isomerase ◽  
Developmental Expression ◽  
Duplicated Genes ◽  
Hordeum Vulgare L ◽  
Disulfide Isomerase ◽  
Genes Encoding ◽  
Encoding Protein ◽  
Protein Disulfide

scholarly journals Nucleotide Sequence of a Wheat cDNA Encoding Protein Disulfide Isomerase

1995 ◽  
Vol 107 (1) ◽  
pp. 281-281 ◽  
Author(s):  
Y. Shimoni ◽  
G. Segal ◽  
Xz. Zhu ◽  
G. Galili
Keyword(s):  
Nucleotide Sequence ◽  
Protein Disulfide Isomerase ◽  
Disulfide Isomerase ◽  
Encoding Protein ◽  
Protein Disulfide

Molecular Cloning of a Fungal cDNA Encoding Protein Disulfide Isomerase

1994 ◽  
Vol 58 (8) ◽  
pp. 1424-1429 ◽  
Author(s):  
Tsutomu Kajino ◽  
Kiyoko Sarai ◽  
Takao Imaeda ◽  
Chie Idekoba ◽  
Osamu Asami ◽  
...  
Keyword(s):  
Molecular Cloning ◽  
Protein Disulfide Isomerase ◽  
Disulfide Isomerase ◽  
Encoding Protein ◽  
Protein Disulfide

scholarly journals Functional Differences in Yeast Protein Disulfide Isomerases

2001 ◽  
Vol 152 (3) ◽  
pp. 553-562 ◽  
Author(s):  
Per Nørgaard ◽  
Vibeke Westphal ◽  
Christine Tachibana ◽  
Lene Alsøe ◽  
Bjørn Holst ◽  
...  
Keyword(s):  
Protein Disulfide Isomerase ◽  
Essential Gene ◽  
Carboxypeptidase Y ◽  
Gene Encoding ◽  
Disulfide Isomerase ◽  
Functional Differences ◽  
Disulfide Isomerases ◽  
Encoding Protein ◽  
Protein Disulfide ◽  
Catalyzed Oxidation

PDI1 is the essential gene encoding protein disulfide isomerase in yeast. The Saccharomyces cerevisiae genome, however, contains four other nonessential genes with homology to PDI1: MPD1, MPD2, EUG1, and EPS1. We have investigated the effects of simultaneous deletions of these genes. In several cases, we found that the ability of the PDI1 homologues to restore viability to a pdi1-deleted strain when overexpressed was dependent on the presence of low endogenous levels of one or more of the other homologues. This shows that the homologues are not functionally interchangeable. In fact, Mpd1p was the only homologue capable of carrying out all the essential functions of Pdi1p. Furthermore, the presence of endogenous homologues with a CXXC motif in the thioredoxin-like domain is required for suppression of a pdi1 deletion by EUG1 (which contains two CXXS active site motifs). This underlines the essentiality of protein disulfide isomerase-catalyzed oxidation. Most mutant combinations show defects in carboxypeptidase Y folding as well as in glycan modification. There are, however, no significant effects on ER-associated protein degradation in the various protein disulfide isomerase-deleted strains.

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