Source:http://linkedlifedata.com/resource/pubmed/id/13678526
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| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
4
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| pubmed:dateCreated |
2003-9-18
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| pubmed:abstractText |
The oxidation and isomerization of disulfide bonds is necessary for the growth of all organisms. In yeast, the oxidative folding of secretory pathway proteins is catalyzed by protein disulfide isomerase (PDI), which requires Ero1p (endoplasmic reticulum oxidoreductin) for its own oxidation. In Homo sapiens, two homologues of Ero1p, Ero1-Lalpha and Ero1-Lbeta, have been cloned. Both Ero1-Lalpha and Ero1-Lbeta interact via disulfide bonds with PDI and support the oxidation of immunoglobulin light chains. However, the function of Ero proteins in plants has not yet been analyzed. In this article, we report the cloning of the two Ero1p homologues present in Arabidopsis thaliana, demonstrating that one of the cDNAs has a shorter terminal exon than predicted and differs from the annotated sequence found in the genome database. Sequence analysis of the Arabidopsis endoplasmic reticulum oxidoreductins (AEROs) reveals that both AERO1 and AERO2 are more closely related to each other than to either of the human Eros. Both in vitro translated AERO proteins are targeted to the endoplasmic reticulum and glycosylated. The ability to use a genetically tractable multicellular organism in combination with biochemical approaches should further our understanding of redox networks and Ero function in both plants and animals.
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| pubmed:language |
eng
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| pubmed:journal | |
| pubmed:citationSubset |
IM
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| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Arabidopsis Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/ERO1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/ERO1L protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Glycoproteins,
http://linkedlifedata.com/resource/pubmed/chemical/Oxidoreductases,
http://linkedlifedata.com/resource/pubmed/chemical/Oxidoreductases Acting on Sulfur...,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins
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| pubmed:status |
MEDLINE
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| pubmed:month |
Aug
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| pubmed:issn |
1523-0864
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| pubmed:author | |
| pubmed:issnType |
Print
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| pubmed:volume |
5
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| pubmed:owner |
NLM
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| pubmed:authorsComplete |
Y
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| pubmed:pagination |
389-96
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| pubmed:dateRevised |
2009-11-19
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| pubmed:meshHeading |
pubmed-meshheading:13678526-Arabidopsis,
pubmed-meshheading:13678526-Arabidopsis Proteins,
pubmed-meshheading:13678526-Base Sequence,
pubmed-meshheading:13678526-Cell Line,
pubmed-meshheading:13678526-Cloning, Molecular,
pubmed-meshheading:13678526-Exons,
pubmed-meshheading:13678526-Genes, Plant,
pubmed-meshheading:13678526-Glycoproteins,
pubmed-meshheading:13678526-Glycosylation,
pubmed-meshheading:13678526-Humans,
pubmed-meshheading:13678526-Introns,
pubmed-meshheading:13678526-Membrane Glycoproteins,
pubmed-meshheading:13678526-Molecular Sequence Data,
pubmed-meshheading:13678526-Oxidoreductases,
pubmed-meshheading:13678526-Oxidoreductases Acting on Sulfur Group Donors,
pubmed-meshheading:13678526-Phylogeny,
pubmed-meshheading:13678526-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:13678526-Sequence Alignment
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| pubmed:year |
2003
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| pubmed:articleTitle |
Cloning and initial characterization of the Arabidopsis thaliana endoplasmic reticulum oxidoreductins.
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| pubmed:affiliation |
Department of Biological and Biomedical Sciences, University of Durham, Durham, U.K.
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| pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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