1. Functional genomics of hsp-90 in parasitic and free-living nematodes
- Author
-
Victoria Gillan, Gillian McCormack, Kirsty Maitland, Eileen Devaney, and Nik A.I.I. Nik Him
- Subjects
Brugia pahangi ,Nematoda ,Molecular Sequence Data ,Mutant ,Helminth genetics ,Article ,03 medical and health sciences ,Haemonchus contortus ,RNA interference ,parasitic diseases ,Animals ,HSP90 Heat-Shock Proteins ,Caenorhabditis elegans ,Gene ,Genes, Helminth ,030304 developmental biology ,Genetics ,Regulation of gene expression ,0303 health sciences ,biology ,fungi ,030302 biochemistry & molecular biology ,Sequence Analysis, DNA ,biology.organism_classification ,Infectious Diseases ,Gene Expression Regulation ,RNAi ,Mutation ,Haemonchus ,Parasitology ,Functional genomics ,Mutant rescue - Abstract
Heat shock protein 90 (Hsp-90) is a highly conserved essential protein in eukaryotes. Here we describe the molecular characterisation of hsp-90 from three nematodes, the free-living Caenorhabditis elegans (Ce) and the parasitic worms Brugia pahangi (Bp) and Haemonchus contortus (Hc). These molecules were functionally characterised by rescue of a Ce-daf-21 (hsp-90) null mutant. Our results show a gradient of rescue: the C. elegans endogenous gene provided full rescue of the daf-21 mutant, while Hc-hsp-90 provided partial rescue. In contrast, no rescue could be obtained using a variety of Bp-hsp-90 constructs, despite the fact that Bp-hsp-90 was transcribed and translated in the mutant worms. daf-21 RNA interference (RNAi) experiments were carried out to determine whether knock-down of the endogenous daf-21 mRNA in N2 worms could be complemented by expression of either parasite gene. However neither parasite gene could rescue the daf-21 (RNAi) phenotypes. These results indicate that factors other than the level of sequence identity are important for determining whether parasite genes can functionally complement in C. elegans.
- Published
- 2009
- Full Text
- View/download PDF