Characterisation of cDNA clones for hypoxanthine-guanine phosphoribosyltransferase from the human malarial parasite, Plasmodium falciparum: comparisons to the mammalian gene and protein.
The isolation of cDNA clones for hypoxanthine-guanine phosphoribosyltransferase (HPRT) from the human malarial parasite, Plasmodium falciparum, is described. Northern analysis indicates that P. falciparum HPRT mRNA is the same size as that coding for mammalian HPRT. The predicted amino acid sequence of the P. falciparum HPRT protein shows extensive homology to the mammalian enzyme. Homology between the two proteins occurs in distinct blocks and a putative catalytic binding domain in the centre of the protein is also conserved. Five out of the seven characterised mammalian HPRT missense mutations map to regions which are conserved in the P. falciparum protein.
King
A
A
Department of Molecular Biology, Edinburgh University, UK.
Melton
D W
DW
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D003001:Cloning, Molecular; D004247:DNA / Q000235:genetics; D005786:Gene Expression Regulation; D005796:Genes; D007041:Hypoxanthine Phosphoribosyltransferase / Q000235:genetics*; D008969:Molecular Sequence Data; D010963:Plasmodium falciparum / Q000235:genetics*; D012333:RNA, Messenger / Q000235:genetics; D014162:Transfection
D012333:RNA, Messenger; D004247:DNA; D007041:Hypoxanthine Phosphoribosyltransferase