Article
In vitro mutagenesis of Caenorhabditis elegans cuticle collagens identifies a potential subtilisin-like protease cleavage site and demonstrates that carboxyl domain disulfide bonding is required for normal function but not assembly.
Molecular and cellular biology - 1 Apr 1994
Yang J, Kramer J M
Abstract excerpt
The importance of conserved amino acids in the amino and carboxyl non-Gly-X-Y domains of Caenorhabditis elegans cuticle collagens was examined by analyzing site-directed mutations of the sqt-1 and rol-6 collagen genes in transgenic animals. Altered collagen genes on transgenic arrays were shown to produce appropriate phenotypes by injecting in vivo cloned mutant alleles. Equivalent alterations in sqt-1 and rol-6...
Topics
- Alleles
- Amino Acid Sequence
- Animals
- Base Sequence
- Caenorhabditis elegans
- Cloning, Molecular
- Collagen
- Conserved Sequence
- Disulfides
- Molecular Sequence Data