Protein disulfide isomerase is essential for viability in Saccharomyces cerevisiae
Identifieur interne : 004909 ( Main/Exploration ); précédent : 004908; suivant : 004910Protein disulfide isomerase is essential for viability in Saccharomyces cerevisiae
Auteurs : Ronnie Farquhar [Royaume-Uni] ; Neville Honey [Royaume-Uni] ; Susan J. Murant [Royaume-Uni] ; Peter Bossier [Royaume-Uni] ; Loren Schultz [Royaume-Uni] ; Donna Montgomery ; Ronald W. Ellis ; Robert B. Freedman [Royaume-Uni] ; Mick F. Tuite [Royaume-Uni]Source :
- Gene [ 0378-1119 ] ; 1991.
English descriptors
- Teeft :
- Active site, Approx, Avian pdis, Biochem, Biological laboratory, Cerevisiae, Clone, Cold spring, Disulfide, Disulfide bond formation, Dohme research laboratories, Ecorv, Fragment, Freedman, Gene, Genomic digests, Higher levels, His3, His3 allele, His3 gene, Isomerase, Mammalian pdis, Mizunaga, Oligo, Oligo probe, Open reading frame, Pdii, Pdii gene, Pdil, Pdil gene, Pdis, Pdiz gene, Physical properties, Polypeptide, Protein disulfide isomerase, Room temperature, Saccharomyces cerevisiae, Secretory, Secretory proteins, Sequence conservation, Single copy gene, Single transcript, Thioredoxin, Tuite, Vertebrate pdis, Viable spores, Yeast, Yeast genome, Yeast genomic library, Yeast pdii gene.
Abstract
Abstract: Protein disulfide isomerase (PDI) is an enzyme involved in the catalysis of disulfide bond formation in secretory and cell-surface proteins. Using an oligodeoxyribonucleotide designed to detect the conserved ‘thioredoxin-like’ active site of vertebrate PDIs, we have isolated a gene encoding PDI from the lower eukaryote, Saccharomyces cerevisiae. The nucleotide sequence and deduced open reading frame of the cloned gene predict a 530-amino-acid (aa) protein of Mr 59082 and a pI of 4.1, physical properties characteristic of mammalian PDIs. Furthermore, the aa sequence shows 30–32% identity with mammalian and avian PDI sequences and has a very similar overall organisation, namely the presence of two approx. 100-aa segments, each of which is repeated, with the most significant homologies to mammalian and avian PDIs being in the regions (a, a') that contain the conserved ‘thioredoxin-like’ active site. The N-terminal region has the characteristics of a cleavable secretory signal sequence and the C-terminal four aa (-His-Asp-Glu-Leu) are consistent with the protein being a component of the S. cerevisiae endoplasmic reticulum. Transformants carrying multiple copies of this gene (designated PDI1) have tenfold higher levels of PDI activity and overproduce a protein of the predicted Mr. The PDI1 gene is unique in the yeast genome and encodes a single 1.8-kb transcript that is not found in stationary phase cells. Disruption of the PDI1 gene is haplo-lethal indicating that the product of this gene is essential for viability.
Url:
DOI: 10.1016/0378-1119(91)90490-3
Affiliations:
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Tuite</name><affiliation></affiliation><affiliation wicri:level="1"><country xml:lang="fr">Royaume-Uni</country><wicri:regionArea>Biological Laboratory, University of Kent, Canterbury, Kent</wicri:regionArea><wicri:noRegion>Kent</wicri:noRegion></affiliation></author></analytic><monogr></monogr><series><title level="j">Gene</title><title level="j" type="abbrev">GENE</title><idno type="ISSN">0378-1119</idno><imprint><publisher>ELSEVIER</publisher><date type="published" when="1991">1991</date><biblScope unit="volume">108</biblScope><biblScope unit="issue">1</biblScope><biblScope unit="page" from="81">81</biblScope><biblScope unit="page" to="89">89</biblScope></imprint><idno type="ISSN">0378-1119</idno></series></biblStruct></sourceDesc><seriesStmt><idno type="ISSN">0378-1119</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="Teeft" xml:lang="en"><term>Active site</term><term>Approx</term><term>Avian pdis</term><term>Biochem</term><term>Biological laboratory</term><term>Cerevisiae</term><term>Clone</term><term>Cold spring</term><term>Disulfide</term><term>Disulfide bond formation</term><term>Dohme research laboratories</term><term>Ecorv</term><term>Fragment</term><term>Freedman</term><term>Gene</term><term>Genomic digests</term><term>Higher levels</term><term>His3</term><term>His3 allele</term><term>His3 gene</term><term>Isomerase</term><term>Mammalian pdis</term><term>Mizunaga</term><term>Oligo</term><term>Oligo probe</term><term>Open reading frame</term><term>Pdii</term><term>Pdii gene</term><term>Pdil</term><term>Pdil gene</term><term>Pdis</term><term>Pdiz gene</term><term>Physical properties</term><term>Polypeptide</term><term>Protein disulfide isomerase</term><term>Room temperature</term><term>Saccharomyces cerevisiae</term><term>Secretory</term><term>Secretory proteins</term><term>Sequence conservation</term><term>Single copy gene</term><term>Single transcript</term><term>Thioredoxin</term><term>Tuite</term><term>Vertebrate pdis</term><term>Viable spores</term><term>Yeast</term><term>Yeast genome</term><term>Yeast genomic library</term><term>Yeast pdii gene</term></keywords></textClass><langUsage><language ident="en">en</language></langUsage></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Abstract: Protein disulfide isomerase (PDI) is an enzyme involved in the catalysis of disulfide bond formation in secretory and cell-surface proteins. Using an oligodeoxyribonucleotide designed to detect the conserved ‘thioredoxin-like’ active site of vertebrate PDIs, we have isolated a gene encoding PDI from the lower eukaryote, Saccharomyces cerevisiae. The nucleotide sequence and deduced open reading frame of the cloned gene predict a 530-amino-acid (aa) protein of Mr 59082 and a pI of 4.1, physical properties characteristic of mammalian PDIs. Furthermore, the aa sequence shows 30–32% identity with mammalian and avian PDI sequences and has a very similar overall organisation, namely the presence of two approx. 100-aa segments, each of which is repeated, with the most significant homologies to mammalian and avian PDIs being in the regions (a, a') that contain the conserved ‘thioredoxin-like’ active site. The N-terminal region has the characteristics of a cleavable secretory signal sequence and the C-terminal four aa (-His-Asp-Glu-Leu) are consistent with the protein being a component of the S. cerevisiae endoplasmic reticulum. Transformants carrying multiple copies of this gene (designated PDI1) have tenfold higher levels of PDI activity and overproduce a protein of the predicted Mr. The PDI1 gene is unique in the yeast genome and encodes a single 1.8-kb transcript that is not found in stationary phase cells. Disruption of the PDI1 gene is haplo-lethal indicating that the product of this gene is essential for viability.</div></front></TEI><affiliations><list><country><li>Royaume-Uni</li></country></list><tree><noCountry><name sortKey="Ellis, Ronald W" sort="Ellis, Ronald W" uniqKey="Ellis R" first="Ronald W." last="Ellis">Ronald W. Ellis</name><name sortKey="Montgomery, Donna" sort="Montgomery, Donna" uniqKey="Montgomery D" first="Donna" last="Montgomery">Donna Montgomery</name></noCountry><country name="Royaume-Uni"><noRegion><name sortKey="Farquhar, Ronnie" sort="Farquhar, Ronnie" uniqKey="Farquhar R" first="Ronnie" last="Farquhar">Ronnie Farquhar</name></noRegion><name sortKey="Bossier, Peter" sort="Bossier, Peter" uniqKey="Bossier P" first="Peter" last="Bossier">Peter Bossier</name><name sortKey="Freedman, Robert B" sort="Freedman, Robert B" uniqKey="Freedman R" first="Robert B." last="Freedman">Robert B. Freedman</name><name sortKey="Honey, Neville" sort="Honey, Neville" uniqKey="Honey N" first="Neville" last="Honey">Neville Honey</name><name sortKey="Murant, Susan J" sort="Murant, Susan J" uniqKey="Murant S" first="Susan J." last="Murant">Susan J. Murant</name><name sortKey="Schultz, Loren" sort="Schultz, Loren" uniqKey="Schultz L" first="Loren" last="Schultz">Loren Schultz</name><name sortKey="Tuite, Mick F" sort="Tuite, Mick F" uniqKey="Tuite M" first="Mick F." last="Tuite">Mick F. Tuite</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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