ArticleThe Biochemical journal1996
Baculovirus expression of two protein disulphide isomerase isoforms from Caenorhabditis elegans and characterization of prolyl 4-hydroxylases containing one of these polypeptides as their beta subunit.
Article in The Biochemical journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
8 citing papers in PubMed, 36 citations in OpenAlex.
- The Redox System in C. elegans, a Phylogenetic Approach.Journal of toxicology · 2012Article
- Article
- Prolyl 4-hydroxylase is an essential procollagen-modifying enzyme required for exoskeleton formation and the maintenance of body shape in the nematode Caenorhabditis elegans.Molecular and cellular biology · 2000Article
- Prolyl 4-hydroxylase is required for viability and morphogenesis in Caenorhabditis elegans.Proceedings of the National Academy of Sciences of the United States of America · 2000Article
- Identification of a novel proline-rich peptide-binding domain in prolyl 4-hydroxylase.The EMBO journal · 1999Article
- The acidic C-terminal domain of protein disulfide isomerase is not critical for the enzyme subunit function or for the chaperone or disulfide isomerase activities of the polypeptide.The EMBO journal · 1999Article
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Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
Protein disulphide isomerase (PDI; EC 5.3.4.1) is a multifunctional polypeptide that is identical to the beta subunit of prolyl 4-hydroxylases. We report here on the cloning and expression of the Caenorhabditis elegans PDI/beta polypeptide and its isoform. The overall amino acid sequence identity and similarity between the processed human and C. elegans PDI/beta polypeptides are 61% and 85% respectively, and those between the C. elegans PDI/beta polypeptide and the PDI isoform 46% and 73%. The isoform differs from the PDI/beta and ERp60 polypeptides in that its N-terminal thioredoxin-like domain has an unusual catalytic site sequence -CVHC-. Expression studies in insect cells demonstrated that the C. elegans PDI/beta polypeptide forms an active prolyl 4-hydroxylase alpha 2 beta 2 tetramer with the human alpha subunit and an alpha beta dimer with the C. elegans alpha subunit, whereas the C. elegans PDI isoform formed no prolyl 4-hydroxylase with either alpha subunit. Removal of the 32-residue C-terminal extension from the C. elegans alpha subunit totally eliminated alpha beta dimer formation. The C. elegans PDI/beta polypeptide formed less prolyl 4-hydroxylase with both the human and C. elegans alpha subunits than did the human PDI/beta polypeptide, being particularly ineffective with the C. elegans alpha subunit. Experiments with hybrid polypeptides in which the C-terminal regions had been exchanged between the human and C. elegans PDI/beta polypeptides indicated that differences in the C-terminal region are one reason, but not the only one, for the differences in prolyl 4-hydroxylase formation between the human and C. elegans PDI/beta polypeptides. The catalytic properties of the C. elegans prolyl 4-hydroxylase alpha beta dimer were very similar to those of the vertebrate type II prolyl 4-hydroxylase tetramer, including the K(m) for the hydroxylation of long polypeptide substrates.
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