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Published August 2010 | public
Journal Article

A vacuolar-type proton (H^+) translocating ATPase α subunit encoded by the Hc-vha-6 gene of Haemonchus contortus

Abstract

In the present study, a full-length cDNA (designated Hc-vha-6) inferred to encode an α subunit of a vacuolar-type proton translocating adenosine triphosphatase (V-ATPase) was isolated from the parasitic nematode Haemonchus contortus, and characterized. The transcript for Hc-vha-6 was detected in all developmental stages and both sexes of H. contortus. Elements, including two TATA box (TATAA), two inverted CAAT box (ATTGG), five E box (CANNTG) and six GATA as well as five inverse GATA (TTATC) transcription factor motifs, were identified in the non-coding region upstream of Hc-vha-6. The open reading frame (ORF) of 2601 nucleotides encoded a protein (Hc-VHA-6) of 866 amino acids and a molecular weight of ~98.7 kDa. Comparison with a published protein sequence for a homologue (VPH1P) from yeast showed that Hc-VHA-6 had nine transmembrane domains and the 14 essential amino acid residues associated with enzyme activity, assembly, intracellular and/or membrane targeting. Phylogenetic analyses of selected amino acid sequence data revealed Hc-VHA-6 to be most closely related to VHA-6 of Caenorhabditis elegans. A predictive network analysis inferred that vha-6 interacts with at least seven other genes encoding V-ATPase subunits and a small Rab GTPase. This study provides the first insight into a V-ATPase of parasitic nematodes and a sound basis for future functional genomic work.

Additional Information

© 2010 Elsevier Ltd. Received 3 January 2010; accepted 22 March 2010. Available online 31 March 2010. Nucleotide sequence data reported in this paper are available in the EMBL, GenBank and DDJB databases under accession numbers FN601335 and FN601336. Funding from the Australian Research Council, the Australian Academy of Science, the Australian-American Fulbright Commission are gratefully acknowledged. PWS is an Investigator with the Howard Hughes Medical Institute.

Additional details

Created:
August 22, 2023
Modified:
October 20, 2023