ArticleMolecular and cellular biology2000
Prolyl 4-hydroxylase is an essential procollagen-modifying enzyme required for exoskeleton formation and the maintenance of body shape in the nematode Caenorhabditis elegans.
Article in Molecular and cellular biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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39 citing papers in PubMed, 114 citations in OpenAlex.
- Calcium-binding protein CALU-1 is essential for proper collagen formation in Caenorhabditis elegans.Cellular and molecular life sciences : CMLS · 2025Article
- Is Exon Skipping a Viable Therapeutic Approach for Vascular Ehlers-Danlos Syndrome with Mutations inInternational journal of molecular sciences · 2024Article
- The Caenorhabditis elegans cuticle and precuticle: a model for studying dynamic apical extracellular matrices in vivo.Genetics · 2024Review
- The proprotein convertase BLI-4 promotes collagen secretion prior to assembly of the Caenorhabditis elegans cuticle.PLoS genetics · 2023Article
- The proprotein convertase BLI-4 promotes collagen secretion during assembly of thebioRxiv : the preprint server for biology · 2023Article
- Defining the filarial N-glycoproteome by glycosite mapping in the human parasitic nematode Brugia malayi.Scientific reports · 2023Article
- Article
- The Arabidopsis Protein Disulfide Isomerase Subfamily M Isoform, PDI9, Localizes to the Endoplasmic Reticulum and Influences Pollen Viability and Proper Formation of the Pollen Exine During Heat Stress.Frontiers in plant science · 2020Article
- Novel Findings of Anti-Filarial Drug Target and Structure-Based Virtual Screening for Drug Discovery.International journal of molecular sciences · 2018Article
- Computational Understanding of the Selectivities in Metalloenzymes.Frontiers in chemistry · 2018Review
- Hydroxylation of Human Type III Collagen Alpha Chain by Recombinant Coexpression with a Viral Prolyl 4-Hydroxylase in Escherichia coli.The protein journal · 2017Article
- Prolyl 4-Hydroxylase: Substrate Isosteres in Which an (E)- or (Z)-Alkene Replaces the Prolyl Peptide Bond.Biochemistry · 2017Article
- Non-neuronal cell outgrowth inWorm · 2017Review
- Molting inWorm · 2017Review
- 4-Fluoroprolines: Conformational Analysis and Effects on the Stability and Folding of Peptides and Proteins.Topics in heterocyclic chemistry · 2017Article
- Article
- The invertebrate Caenorhabditis elegans biosynthesizes ascorbate.Archives of biochemistry and biophysics · 2015Article
- Enzymology of the nematode cuticle: A potential drug target?International journal for parasitology. Drugs and drug resistance · 2014Review
- Biological safety of fish (tilapia) collagen.BioMed research international · 2014Article
- Bioavailable affinity label for collagen prolyl 4-hydroxylase.Bioorganic & medicinal chemistry · 2013Article
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The multienzyme complex prolyl 4-hydroxylase catalyzes the hydroxylation of proline residues and acts as a chaperone during collagen synthesis in multicellular organisms. The beta subunit of this complex is identical to protein disulfide isomerase (PDI). The free-living nematode Caenorhabditis elegans is encased in a collagenous exoskeleton and represents an excellent model for the study of collagen biosynthesis and extracellular matrix formation. In this study, we examined prolyl 4-hydroxylase alpha-subunit (PHY; EC 1.14.11.2)- and beta-subunit (PDI; EC 5.3.4.1)-encoding genes with respect to their role in collagen modification and formation of the C. elegans exoskeleton. We identified genes encoding two PHYs and a single associated PDI and showed that all three are expressed in collagen-synthesizing ectodermal cells at times of maximal collagen synthesis. Disruption of the pdi gene via RNA interference resulted in embryonic lethality. Similarly, the combined phy genes are required for embryonic development. Interference with phy-1 resulted in a morphologically dumpy phenotype, which we determined to be identical to the uncharacterized dpy-18 locus. Two dpy-18 mutant strains were shown to have null alleles for phy-1 and to have a reduced hydroxyproline content in their exoskeleton collagens. This study demonstrates in vivo that this enzyme complex plays a central role in extracellular matrix formation and is essential for normal metazoan development.
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