<scp>III</scp>. Yeast sequencing reports. Determination of the sequence of the yeast <i>YCL313</i> gene localized on chromosome III. Homology with the protein disulfide isomerase (PDI gene product) of other organisms

Scherens, Bart; Dubois, Evelyne; Messenguy, Francine

doi:10.1002/yea.320070212

Cited by 57 publications

(49 citation statements)

References 39 publications

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“…PDI is a catalyst of the rate-limiting reactions of disulphide-bond formation, isomerization and reduction within the ER [8], and it displays chaperone activity (described below) in itro and in i o. In Saccharomyces cere isiae PDI is an indispensable protein [15], and its essential role in this organism has been shown to be the isomerization of disulphide bonds [16], although this issue has been disputed for some time. Association between PDI and malfolded proteins (such as overexpressed lysozyme mutants) or endogenous, nascent proteins (e.g.…”

Section: Pdimentioning

confidence: 99%

“…The fact that PDI is an essential protein in S. cere isiae [15] (see below), where its critical role is the isomerization of disulphide bonds [16] rather than its redox properties, further highlights the importance of investigating the role of the b\bh domains in PDI function. Finally, it may be of importance that the b\bh domains of PDI are a target for phosphorylation and may even catalyse ATP hydrolysis, which increases upon binding of peptides but not during redox reactions [73,74].…”

Section: Scheme 1 Possible Mechanisms Of Disulphide-bond Formation Rmentioning

confidence: 99%

“…PDI is essential for the viability of S. cere isiae [15,[75][76][77][78], and its essential role is in the isomerization of disulphide bonds [16,38], although its redox activity is clearly important for substrates such as carboxypeptidase Y [79]. Mammalian PDI can rescue PDI-deficient yeast, despite only low sequence identity (30 %) between the two proteins [81].…”

Section: Pdi-deficient Yeast Strains and The Maturation Of Carboxypepmentioning

confidence: 99%

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The protein disulphide-isomerase family: unravelling a string of folds

Ferrari

Söling

1999

Biochemical Journal

405

359

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The mammalian protein disulphide-isomerase (PDI) family encompasses several highly divergent proteins that are involved in the processing and maturation of secretory proteins in the endoplasmic reticulum. These proteins are characterized by the presence of one or more domains of roughly 95-110 amino acids related to the cytoplasmic protein thioredoxin. All but the PDI-D subfamily are composed entirely of repeats of such domains, with at least one domain containing and one domain lacking a redox-active -Cys-Xaa-Xaa-Cys-tetrapeptide. In addition to their known roles as redox catalysts and isomerases, the last few years have revealed additional functions of the PDI proteins,

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Section: Pdimentioning

confidence: 99%

Section: Scheme 1 Possible Mechanisms Of Disulphide-bond Formation Rmentioning

confidence: 99%

Section: Pdi-deficient Yeast Strains and The Maturation Of Carboxypepmentioning

confidence: 99%

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The protein disulphide-isomerase family: unravelling a string of folds

Ferrari

Söling

1999

Biochemical Journal

405

359

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“…The core pathway contains two conserved proteins: Pdi1p and Ero1p. Protein disulfide isomerase (PDI) catalyzes formation, isomerization, and reduction of disulfide bonds of substrate proteins (18,22,23,33). The ER membrane-associated protein Ero1p (ER oxidoreduction) introduces oxidizing equivalents through a flavin-dependent mechanism, engaging thiol-disulfide exchange with Pdi1p (17,38).…”

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confidence: 99%

Secretion of Human Serum Albumin by Kluyveromyces lactis Overexpressing KlPDI1 and KlERO1

Lodi

Neglia

Donnini

2005

Appl Environ Microbiol

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The control of protein conformation during translocation through the endoplasmic reticulum is often a bottleneck for heterologous protein production. The core pathway of the oxidative folding machinery includes two conserved proteins: Pdi1p and Ero1p. We increased the dosage of the genes encoding these proteins in the yeast Kluyveromyces lactis and evaluated the secretion of heterologous proteins. KlERO1, an orthologue of Saccharomyces cerevisiae ERO1, was cloned by functional complementation of the ts phenotype of an Scero1 mutant. The expression of KlERO1 was induced by treatment of the cells with dithiothreitol and by overexpression of human serum albumin (HSA), a disulfide bond-rich protein. Duplication of either PDI1 or ERO1 led to a similar increase in HSA yield. Duplication of both genes accelerated the secretion of HSA and improved cell growth rate and yield. Increasing the dosage of KlERO1 did not affect the production of human interleukin 1␤, a protein that has no disulfide bridges. The results confirm that the ERO1 genes of S. cerevisiae and K. lactis are functionally similar even though portions of their coding sequence are quite different and the phenotypes of mutants overexpressing the genes differ. The marked effects of KlERO1 copy number on the expression of heterologous proteins with a high number of disulfide bridges suggests that control of KlERO1 and KlPDI1 is important for the production of high levels of heterologous proteins of this type.In eukaryotes, the specific folding of proteins targeted to the secretory pathway or to extracellular space occurs in the endoplasmic reticulum (ER). For many secretory proteins, the proper folding requires the formation of intra-and intermolecular disulfide bonds (for reviews, see references 15, 21, and 39). The pathway of oxidative protein folding has been extensively studied in Saccharomyces cerevisiae. Genes have been identified that are involved in redox homeostasis within the ER. The protein folding process requires numerous chaperones and enzymes. The core pathway contains two conserved proteins: Pdi1p and Ero1p. Protein disulfide isomerase (PDI) catalyzes formation, isomerization, and reduction of disulfide bonds of substrate proteins (18,22,23,33). The ER membrane-associated protein Ero1p (ER oxidoreduction) introduces oxidizing equivalents through a flavin-dependent mechanism, engaging thiol-disulfide exchange with Pdi1p (17,38). Mutations in ERO1 and PDI1 result in cells that are sensitive to the reducing agent dithiothreitol (DTT) and that accumulate proteins that normally contain disulfide bonds in reduced form in the ER. The accumulation of reduced proteins induces the unfolded protein response (16,19,29,30). Overexpression of ERO1 results in cells resistant to DTT (16). A few other proteins functionally related to Pdi1p or to Ero1p have also been identified in S. cerevisiae. Overproduction of Mpd1, Mpd2, Eug1, and Eps1 can partially complement the loss of Pdi1p, and overproduction of Erv2 partially complements the loss of Ero1. Unlike ERO1 a...

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“…We were interested in examining the role of disulfide bond formation in protein transport and protein sorting in the yeast secretory pathway. An essential gene encoding yeast PDI (PDIH) has been previously characterized (19,25,38,54). We report here the cloning of a yeast gene (EUGI) that is homologous to PDIL.…”

mentioning

confidence: 99%

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

Tachibana¹,

Stevens²

1992

Mol. Cell. Biol.

145

130

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The product of the EUGI gene of Saccharomyces cerevisiae is a soluble endoplasmic reticulum protein with homology to both the mammalian protein disulfide isomerase (PDI) Protein translocation across membranes requires that proteins assume an unfolded conformation (8, 13). Proteins entering the secretory pathway are translocated across the endoplasmic reticulum (ER) membrane, and these newly synthesized proteins assume their native conformation prior to export from the ER (9, 22). Interactions between the nascent, folding polypeptides and resident ER proteins may aid in newly synthesized proteins achieving a native conformation (23). Proposed interactions include binding to BiP to prevent aggregation and to promote folding and oligomerization (22, 41) and isomerization by protein disulfide isomerase (PDI) to assist in the formation of native disulfide bonds (20, 24).Many secretory proteins undergo disulfide bond formation in the oxidizing environment of the ER lumen. Several lines of evidence suggest that PDI participates in the folding of proteins containing disulfide bonds. PDI was originally characterized for its ability to catalyze the steps in the in vitro refolding of RNase A (24), bovine pancreatic trypsin inhibitor (10), and collagen (35), all of which require disulfide bond rearrangements. More recently, it was demonstrated that ER microsomes depleted of PDI by a high-pH wash were able to translocate and glycosylate -y-

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III. Yeast sequencing reports. Determination of the sequence of the yeast YCL313 gene localized on chromosome III. Homology with the protein disulfide isomerase (PDI gene product) of other organisms

Cited by 57 publications

References 39 publications

The protein disulphide-isomerase family: unravelling a string of folds

The protein disulphide-isomerase family: unravelling a string of folds

Secretion of Human Serum Albumin by Kluyveromyces lactis Overexpressing KlPDI1 and KlERO1

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

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