Constitutive overexpression of secreted heterologous proteins decreases extractable heavy chain binding protein and protein disulfide isomerase levels in Saccharomyces cerevisiae

1995 ◽  
Vol 11 (2) ◽  
pp. 171-177 ◽  
Author(s):  
Anne Skaja Robinson ◽  
K. Dane Wittrup
1992 ◽  
Vol 12 (10) ◽  
pp. 4601-4611
Author(s):  
C Tachibana ◽  
T H Stevens

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.


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

2009 ◽  
Vol 3 (1) ◽  
pp. 27-32
Author(s):  
PURKAN PURKAN ◽  
LALU RUDYAT TELLY SAVALAS ◽  
MULIAWATI SINDUMARTA ◽  
DESSY NATALIA

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

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