- page settings
- showhide sidebar
- showhide empty fields
- layout
- (too narrow)
- open all
- close all
- Page Content
- Overview
- External Links
- History
- Referenced
- Tools
- Tree Display
- My WormBase
- My Favorites
- My Library
- Recent Activity
- Comments (0)
history logging is off
Tree Display
My Favorites
My Library
Comments on Gerrits D et al. (1996) European Worm Meeting "TYROSINASES OF CAENORHABDITIS ELEGANS" (0)
Overview
Gerrits D, & Blaxter ML (1996). TYROSINASES OF CAENORHABDITIS ELEGANS presented in European Worm Meeting. Unpublished information; cite only with author permission.
The cuticle of C. elegans is extensively cross-linked by covalent disulphide bridges, tyrosine bonds and possibly glutamyl-lysine bonds. Two enzymes presumably involved in the formation of tyrosine bonds have been identified in C. elegans. Both genes map to chromosome III. tyr-1 and tyr-2 appear to be very similar in structure: both genes have two Cu active sites (CuA and CuB) and two NC6 domains (found in other proteins from C. elegans and Toxocara canis ). tyr-1 has an additional polyglutamine region which may be involved in protein-protein interactions. A set of cDNA's prepared from a synchronous population of worms, harvested at two hour intervals through the lifecycle, starting shortly after hatching (cDNA kindly provided by I. Johnstone), was used in semi-quantitative fluorescent PCR. Preliminary results suggest that both genes are upregulated at each moult, suggesting their involvement in the synthesis of the new cuticle. Different parts of both genes have been cloned and expressed in E. coli. Antibodies against these recombinant proteins were raised in mice and will be used to locate the native proteins in worms.
Affiliation:
- University of Edinburgh, ICAPB, Ashworth laboratories, King's buildings, West Mains road, Edinburgh, EH9 3JT