We report the nucleotide and derived amino acid sequence of the ATPase 1 gene from Plasmodium falciparum. The amino acid sequence shares homology with the family of "P"-type cation translocating ATPases in conserved regions important for nucleotide binding, conformational change, or phosphorylation. The gene, which is present on chromosome 5, has a product longer than any other reported for a P-type ATPase. Interstrain analysis from 12 parasite isolates by the polymerase chain reaction reveals that a 330-bp nucleotide sequence encoding three cytoplasmic regions conserved in cation ATPases (regions a-c) is of constant length. By contrast, another 360-bp sequence which is one of four regions we refer to as "inserts" contains arrays of tandem repeats which show length variation between different parasite isolates. Polymorphism results from differences in the number and types of repeat motif contained in this insert. Inserts are divergent in sequence from other P-type ATPases and share features in common with many malarial antigens. Studies using RNA from the erythrocytic stages of the malarial life cycle suggest that ATPase 1 (including the sequence which encodes tandem repeats) is expressed at the large ring stage of development. Immunolocalization has identified ATPase 1 to be in the region of the parasite plasma membrane and pigment body. These findings suggest a possible model for the genesis of malarial antigens.
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15 January 1993
Article|
January 15 1993
A family of cation ATPase-like molecules from Plasmodium falciparum.
S Krishna,
S Krishna
Medical Research Council Molecular Haematology Unit, John Radcliffe Hospital, Oxford, United Kingdom.
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G Cowan,
G Cowan
Medical Research Council Molecular Haematology Unit, John Radcliffe Hospital, Oxford, United Kingdom.
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J C Meade,
J C Meade
Medical Research Council Molecular Haematology Unit, John Radcliffe Hospital, Oxford, United Kingdom.
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R A Wells,
R A Wells
Medical Research Council Molecular Haematology Unit, John Radcliffe Hospital, Oxford, United Kingdom.
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J R Stringer,
J R Stringer
Medical Research Council Molecular Haematology Unit, John Radcliffe Hospital, Oxford, United Kingdom.
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K J Robson
K J Robson
Medical Research Council Molecular Haematology Unit, John Radcliffe Hospital, Oxford, United Kingdom.
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S Krishna
Medical Research Council Molecular Haematology Unit, John Radcliffe Hospital, Oxford, United Kingdom.
G Cowan
Medical Research Council Molecular Haematology Unit, John Radcliffe Hospital, Oxford, United Kingdom.
J C Meade
Medical Research Council Molecular Haematology Unit, John Radcliffe Hospital, Oxford, United Kingdom.
R A Wells
Medical Research Council Molecular Haematology Unit, John Radcliffe Hospital, Oxford, United Kingdom.
J R Stringer
Medical Research Council Molecular Haematology Unit, John Radcliffe Hospital, Oxford, United Kingdom.
K J Robson
Medical Research Council Molecular Haematology Unit, John Radcliffe Hospital, Oxford, United Kingdom.
Online ISSN: 1540-8140
Print ISSN: 0021-9525
J Cell Biol (1993) 120 (2): 385–398.
Citation
S Krishna, G Cowan, J C Meade, R A Wells, J R Stringer, K J Robson; A family of cation ATPase-like molecules from Plasmodium falciparum.. J Cell Biol 15 January 1993; 120 (2): 385–398. doi: https://doi.org/10.1083/jcb.120.2.385
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