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A more recent version of this article appeared on April 1, 2003
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Submitted on August 9, 2002
Revised on December 9, 2002
Accepted on December 23, 2002
1 The Wellcome Centre for Molecular Parasitology, The University of Glasgow, Anderson College, 56 Dumbarton Rd., Glasgow, G11 6NU, UK (present address: Invitrogen Ltd, 3 Fountain Drive, Inchinnan Business Park, Paisley, PA4 9RF, UK)
2 The Wellcome Centre for Molecular Parasitology, The University of Glasgow, Anderson College, 56 Dumbarton Rd., Glasgow, G11 6NU, UK (present address: Northwestern University Medical School, Dept. of Cell and Molecular Biology, 303 E. Chicago Ave., Chicago, IL 60611)
3 The Wellcome Centre for Molecular Parasitology, The University of Glasgow, Anderson College, 56 Dumbarton Rd., Glasgow, G11 6NU, UK
* Corresponding author. E-mail address: i.johnstone{at}vet.gla.ac.uk.
A ubiquitous feature of collagens is protein interaction, the trimerisation of monomers to form a triple helix followed by higher order interactions during the formation of the mature extracellular matrix (ECM). The Caenorhabditis elegans cuticle is a complex ECM consisting predominantly of cuticle collagens, which are encoded by a family of approximately 154 genes. We identify two discrete interacting sets of collagens and show that they form functionally distinct matrix sub-structures. We show that mutation in or RNA-mediated interference of a gene encoding a collagen belonging to one interacting set affects the assembly of other members of that set, but not those belonging to the other set. During cuticle synthesis, the collagen genes are expressed in a distinct temporal series which we hypothesize exists to facilitate partner finding and the formation of appropriate interactions between encoded collagens. Consistent with this, we find for the two identified interacting sets that the individual members of each set are temporally co-expressed, whereas the two sets are expressed approximately two hours apart during matrix synthesis.
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