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genetics.105.053637v1
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doi:10.1534/genetics.105.053637
A more recent version of this article appeared on April 1, 2006.
REGULAR RESEARCH PAPERS |
The C-terminus of collagen SQT-3 has complex and essential functions in nematode collagen assembly
Jacopo Novelli 1, Antony Page 2 and Jonathan Hodgkin 1*
1 University of Oxford
2 Glasgow University
* To whom correspondence should be addressed. E-mail: jah{at}bioch.ox.ac.uk.
Submitted on November 17, 2005
Revised on December 27, 2005
Accepted on 16 January 2006
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, extensively redundant 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 between 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 non-trimeric 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.
Key Words: BMP-1 homolog, Collagen assembly, Nematode, temperature sensitivity
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