Functional genomics of hsp-90 in parasitic and free-living nematodes.
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.
Gillan
Victoria
V
Parasitology Group, Division of Infection and Immunity, Institute of Comparative Medicine, Faculty of Veterinary Medicine, University of Glasgow, Bearsden Road, Glasgow G61 1QH, UK. v.gillan@vet.gla.ac.uk
Maitland
Kirsty
K
McCormack
Gillian
G
Him
Nik A I I Nik
NA
Devaney
Eileen
E
D000818:Animals; D017179:Brugia pahangi / Q000235:genetics; D017173:Caenorhabditis elegans / Q000235:genetics; D005786:Gene Expression Regulation / Q000235:genetics*; D017238:Genes, Helminth / Q000235:genetics*; D018841:HSP90 Heat-Shock Proteins / Q000235:genetics* / Q000378:metabolism; D006189:Haemonchus / Q000235:genetics; D008969:Molecular Sequence Data; D009154:Mutation; D009348:Nematoda / Q000235:genetics* / Q000469:parasitology; D017422:Sequence Analysis, DNA
D018841:HSP90 Heat-Shock Proteins