scholarly journals The b’x Region of Yeast Protein Disulfide Isomerase is Not Essential for Saccharomyces cerevisiae Viability at 30 °C

2009 ◽  
Vol 3 (1) ◽  
pp. 27-32
Author(s):  
PURKAN PURKAN ◽  
LALU RUDYAT TELLY SAVALAS ◽  
MULIAWATI SINDUMARTA ◽  
DESSY NATALIA
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Protein Disulfide Isomerase ◽  
Yeast Protein ◽  
Disulfide Isomerase ◽  
Protein Disulfide

The yeast EUG1 gene encodes an endoplasmic reticulum protein that is functionally related to protein disulfide isomerase

1992 ◽  
Vol 12 (10) ◽  
pp. 4601-4611
Author(s):  
C Tachibana ◽  
T H Stevens
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Endoplasmic Reticulum ◽  
Protein Disulfide Isomerase ◽  
Yeast Cells ◽  
Disulfide Isomerase ◽  
Protein Levels ◽  
Growth Defects ◽  
Endoplasmic Reticulum Protein ◽  
Related Proteins ◽  
Protein Disulfide

The product of the EUG1 gene of Saccharomyces cerevisiae is a soluble endoplasmic reticulum protein with homology to both the mammalian protein disulfide isomerase (PDI) and the yeast PDI homolog encoded by the essential PDI1 gene. Deletion or overexpression of EUG1 causes no growth defects under a variety of conditions. EUG1 mRNA and protein levels are dramatically increased in response to the accumulation of native or unglycosylated proteins in the endoplasmic reticulum. Overexpression of the EUG1 gene allows yeast cells to grow in the absence of the PDI1 gene product. Depletion of the PDI1 protein in Saccharomyces cerevisiae causes a soluble vacuolar glycoprotein to accumulate in its endoplasmic reticulum form, and this phenotype is only partially relieved by the overexpression of EUG1. Taken together, our results indicate that PDI1 and EUG1 encode functionally related proteins that are likely to be involved in interacting with nascent polypeptides in the yeast endoplasmic reticulum.

Functional differences between human and yeast protein disulfide isomerase family proteins

2004 ◽  
Vol 320 (2) ◽  
pp. 359-365 ◽  
Author(s):  
Taiji Kimura ◽  
Yasuhiro Hosoda ◽  
Yukiko Kitamura ◽  
Hideshi Nakamura ◽  
Tomohisa Horibe ◽  
...  
Keyword(s):  
Protein Disulfide Isomerase ◽  
Yeast Protein ◽  
Disulfide Isomerase ◽  
Functional Differences ◽  
Protein Disulfide ◽  
Protein Disulfide Isomerase Family

Production of Rat Protein Disulfide Isomerase in Saccharomyces cerevisiae

1995 ◽  
Vol 6 (5) ◽  
pp. 700-706 ◽  
Author(s):  
M.C.A. Laboissiere ◽  
P.T. Chivers ◽  
R.T. Raines
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Protein Disulfide Isomerase ◽  
Disulfide Isomerase ◽  
Protein Disulfide

Protein disulfide isomerase is essential for viability in Saccharomyces cerevisiae

Gene ◽  
1991 ◽  
Vol 108 (1) ◽  
pp. 81-89 ◽  
Author(s):  
Ronnie Farquhar ◽  
Neville Honey ◽  
Susan J. Murant ◽  
Peter Bossier ◽  
Loren Schultz ◽  
...  
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Protein Disulfide Isomerase ◽  
Disulfide Isomerase ◽  
Protein Disulfide

scholarly journals Htm1p–Pdi1p is a folding-sensitive mannosidase that marks N-glycoproteins for ER-associated protein degradation

2016 ◽  
Vol 113 (28) ◽  
pp. E4015-E4024 ◽  
Author(s):  
Yi-Chang Liu ◽  
Danica Galonić Fujimori ◽  
Jonathan S. Weissman
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Endoplasmic Reticulum ◽  
Protein Degradation ◽  
Protein Disulfide Isomerase ◽  
Misfolded Proteins ◽  
Disulfide Isomerase ◽  
Licensing Factor ◽  
Folded Proteins ◽  
Protein Disulfide

Our understanding of how the endoplasmic reticulum (ER)-associated protein degradation (ERAD) machinery efficiently targets terminally misfolded proteins while avoiding the misidentification of nascent polypeptides and correctly folded proteins is limited. For luminal N-glycoproteins, demannosylation of their N-glycan to expose a terminal α1,6-linked mannose is necessary for their degradation via ERAD, but whether this modification is specific to misfolded proteins is unknown. Here we report that the complex of the mannosidase Htm1p and the protein disulfide isomerase Pdi1p (Htm1p–Pdi1p) acts as a folding-sensitive mannosidase for catalyzing this first committed step in Saccharomyces cerevisiae. We reconstitute this step in vitro with Htm1p–Pdi1p and model glycoprotein substrates whose structural states we can manipulate. We find that Htm1p–Pdi1p is a glycoprotein-specific mannosidase that preferentially targets nonnative glycoproteins trapped in partially structured states. As such, Htm1p–Pdi1p is suited to act as a licensing factor that monitors folding in the ER lumen and preferentially commits glycoproteins trapped in partially structured states for degradation.

scholarly journals Construction of a Library of Human Glycosyltransferases Immobilized in the Cell Wall of Saccharomyces cerevisiae

2006 ◽  
Vol 72 (11) ◽  
pp. 7003-7012 ◽  
Author(s):  
Yoh-ichi Shimma ◽  
Fumie Saito ◽  
Fumi Oosawa ◽  
Yoshifumi Jigami
Keyword(s):  
Saccharomyces Cerevisiae ◽  
Cell Wall ◽  
Yeast Cell ◽  
Protein Disulfide Isomerase ◽  
Immobilized Enzymes ◽  
Enzymatic Activities ◽  
Yeast Cell Wall ◽  
Yeast Protein ◽  
A Cell ◽  
Protein Disulfide

ABSTRACT Fifty-one human glycosyltransferases were expressed in Saccharomyces cerevisiae as immobilized enzymes and were assayed for enzymatic activities. The stem and catalytic regions of sialyl-, fucosyl-, galactosyl-, N-acetylgalactosaminyl-, and N-acetylglucosaminyltransferases were fused with yeast cell wall Pir proteins, which anchor glycosyltransferases at the yeast cell wall glucan. More than 75% of expressed recombinant glycosyltransferases retained their enzymatic activities in the yeast cell wall fraction and will be used as a human glycosyltransferase library. In increasing the enzymatic activities of immobilized glycosyltransferases, several approaches were found to be effective. Additional expression of yeast protein disulfide isomerase increased the expression levels and activities of polypeptide N-acetylgalactosaminyltransferases and other glycosyltransferases. PIR3 and/or PIR4 was more effective than PIR1 as a cell wall anchor when the Pir-glycosyltransferase fusions were expressed under the control of the constitutive glyceraldehyde-3-phosphate dehydrogenase promoter. Oligosaccharides such as Lewis x, Lewis y, and H antigen were successfully synthesized using this immobilized glycosyltransferase library, indicating that the Pir-fused glycosyltransferases are useful for the production of various human oligosaccharides.

scholarly journals Interactions among Yeast Protein-Disulfide Isomerase Proteins and Endoplasmic Reticulum Chaperone Proteins Influence Their Activities

2005 ◽  
Vol 280 (36) ◽  
pp. 31438-31441 ◽  
Author(s):  
Taiji Kimura ◽  
Yasuhiro Hosoda ◽  
Yoshimi Sato ◽  
Yukiko Kitamura ◽  
Takezo Ikeda ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Protein Disulfide Isomerase ◽  
Chaperone Proteins ◽  
Yeast Protein ◽  
Disulfide Isomerase ◽  
Endoplasmic Reticulum Chaperone ◽  
Protein Disulfide
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