| The C terminus of collagen SQT-3 has complex and essential functions in nematode collagen assembly. | |
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MedLine Citation:
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PMID: 16452136 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The nematode exoskeleton is a multilayered structure secreted by the underlying hypodermal cells and mainly composed of small collagens, which are encoded by a large gene family. In previous work, we reported analysis of the C. elegans dpy-31 locus, encoding a hypodermally expressed zinc-metalloprotease of the BMP-1/TOLLOID family essential for viability and cuticle deposition. We have generated a large set of extragenic suppressors of dpy-31 lethality, most of which we show here to be allelic to the cuticle collagen genes sqt-3 and dpy-17. We analyzed the interaction among dpy-31, sqt-3, and dpy-17 using a SQT-3-specific antiserum, which was employed in immunofluorescence experiments. Our results support a role for DPY-31 in SQT-3 extracellular processing and suggest that the SQT-3 C-terminal nontrimeric region serves multiple roles during SQT-3 assembly. Different missense mutations of this region have diverse phenotypic consequences, including cold-sensitive lethality. Furthermore, the biochemical and genetic data indicate that the extracellular assemblies of DPY-17 and SQT-3 are interdependent, most likely because the collagens are incorporated into the same cuticular substructure. We find that absence of DPY-17 causes extensive intracellular retention of SQT-3, indicating that formation of the SQT-3-DPY-17 polymer could begin in the intracellular environment before secretion. |
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Authors:
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Jacopo Novelli; Antony P Page; Jonathan Hodgkin |
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Publication Detail:
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Type: Journal Article Date: 2006-02-01 |
Journal Detail:
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Title: Genetics Volume: 172 ISSN: 0016-6731 ISO Abbreviation: Genetics Publication Date: 2006 Apr |
Date Detail:
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Created Date: 2006-04-25 Completed Date: 2006-07-17 Revised Date: 2009-11-18 |
Medline Journal Info:
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Nlm Unique ID: 0374636 Medline TA: Genetics Country: United States |
Other Details:
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Languages: eng Pagination: 2253-67 Citation Subset: IM |
Affiliation:
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Genetics Unit, Department of Biochemistry, University of Oxford, United Kingdom. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Alleles Amino Acid Sequence Animals Caenorhabditis elegans Caenorhabditis elegans Proteins / chemistry*, metabolism Chromosome Mapping Cloning, Molecular Collagen / chemistry* Helminth Proteins / metabolism Metalloendopeptidases / metabolism Microscopy, Fluorescence Models, Genetic Molecular Sequence Data Mutation, Missense Non-Fibrillar Collagens Polymers / chemistry Protein Structure, Tertiary Transgenes |
| Chemical | |
Reg. No./Substance:
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0/Caenorhabditis elegans Proteins; 0/Helminth Proteins; 0/Non-Fibrillar Collagens; 0/Polymers; 0/SQT-3 protein, C elegans; 0/dpy-17 protein, C elegans; 9007-34-5/Collagen; EC 3.4.-/DPY-31 protein, C elegans; EC 3.4.24.-/Metalloendopeptidases |
| Comments/Corrections | |
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