Document Detail


The C terminus of collagen SQT-3 has complex and essential functions in nematode collagen assembly.
MedLine Citation:
PMID:  16452136     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
Jacopo Novelli; Antony P Page; Jonathan Hodgkin
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Publication Detail:
Type:  Journal Article     Date:  2006-02-01
Journal Detail:
Title:  Genetics     Volume:  172     ISSN:  0016-6731     ISO Abbreviation:  Genetics     Publication Date:  2006 Apr 
Date Detail:
Created Date:  2006-04-25     Completed Date:  2006-07-17     Revised Date:  2014-02-19    
Medline Journal Info:
Nlm Unique ID:  0374636     Medline TA:  Genetics     Country:  United States    
Other Details:
Languages:  eng     Pagination:  2253-67     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
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
Grant Support
ID/Acronym/Agency:
G0000114//Medical Research Council; G117/476//Medical Research Council
Chemical
Reg. No./Substance:
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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