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Vol. 14, Issue 4, 1366-1378, April 2003
The Wellcome Centre for Molecular Parasitology, The
University of Glasgow, Anderson College, Glasgow G11 6NU, United
Kingdom
A ubiquitous feature of collagens is protein interaction, the
trimerization of monomers to form a triple helix followed by higher
order interactions during the formation of the mature extracellular matrix. The Caenorhabditis elegans cuticle is a
complex extracellular matrix consisting predominantly of cuticle
collagens, which are encoded by a family of ~154 genes. We identify
two discrete interacting sets of collagens and show that they form
functionally distinct matrix substructures. 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 hypothesis, we find for the two identified interacting sets that
the individual members of each set are temporally coexpressed, whereas
the two sets are expressed ~2 h apart during matrix synthesis.
Online version of this article contains supplementary data.
Online version is available at www.molbiolcell.org.
Present addresses:
*Invitrogen Ltd, 3 Fountain Dr., Inchinnan Business
Park, Paisley, PA4 9RF, United Kingdom;
Department of
Cell and Molecular Biology, Northwestern University Medical School, 303 E. Chicago Ave., Chicago, IL 60611.
Corresponding author. E-mail address:
i.johnstone{at}vet.gla.ac.uk.
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