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Mol Biochem Parasitol. 1996 Jun;78(1-2):1-12.

Analysis of a cation-transporting ATPase of Plasmodium falciparum.

Author information

1
Department of Zoology, University of Oxford, UK. mike.dyer@zoology.oxford.ac.uk

Abstract

We have cloned and characterised one gene, PfATPase4 which encodes a P-type ATPase containing all the primary sequence motifs characteristic of this class of transmembrane ion transporters, and also a fragment of a second P. falciparum P-type ATPase pseudogene (PfATPase5). Analysis of conserved domains and motifs of specific ATPases reveals that PfATPase4 is most analogous to Ca2+ ATPases of the endoplasmic reticulum. The PfATPase4 gene gives rise to a transcript of 8 kb shortly after erythrocyte invasion. Although this mRNA is not detected in later stages, the protein detected immunologically at 190 kDa persists throughout and is detected in free merozoites. Immunofluorescence microscopy reveals that the PfATPase4 protein is concentrated in discrete compartments at the periphery of the parasite. Detailed sequence and structural analyses of these and the other P-type ATPases of P. falciparum described previously, reveals that they comprise an unusual family in several respects. Firstly, the large number of non-homologous genes so far characterised reflects the complexities of ionic regulation in the diverse environments encountered by the parasite. Secondly, the plasmodial P-type ATPase family may be classified both at primary sequence and structural levels into two distinct groups-those typical of P-type ATPases (including PfATPase4) and those which are much more divergent. A third complexity is illustrated by the fact that one of the other members [1] here termed PfATPase6, has an even greater similarity to the sarcoplasmic reticulum Ca2+ ATPases than does PfATPase4, which raises questions about the possible functional relationship between these two members.

PMID:
8813672
DOI:
10.1016/s0166-6851(96)02593-5
[Indexed for MEDLINE]

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