Aspartyl proteinase genes from apicomplexan parasites: evidence for evolution of the gene structure.
Aspartyl proteinases are a widely distributed family of enzymes. All vertebrate aspartyl proteinases share a conserved nine-exon gene structure, but in other organisms the structure of aspartyl proteinase genes varies considerably. The exon-intron patterns generally reflect phylogeny based on amino acid sequences. However, close comparison of these gene structures reveals some striking features, such as the conservation of intron positions and intron phases between aspartyl proteinases from nematodes and apicomplexans. Here, we discuss the implications of gene structure for the possible evolution of the aspartyl proteinase family, with particular reference to the plasmepsins of Plasmodium falciparum and eimepsin from Eimeria tenella.
Jean
L
L
National Institute for Medical Research, Division of Parasitology, The Ridgeway, Mill Hill, London, UK NW7 1AA. ljean@nimr.mrc.ac.uk
Long
M
M
Young
J
J
Péry
P
P
Tomley
F
F
D000595:Amino Acid Sequence; D000818:Animals; D016782:Apicomplexa / Q000201:enzymology* / Q000235:genetics; D016282:Aspartic Acid Endopeptidases / Q000737:chemistry / Q000235:genetics*; D016786:Eimeria tenella / Q000201:enzymology / Q000235:genetics; D019143:Evolution, Molecular; D017125:Genes, Protozoan; D008969:Molecular Sequence Data; D010963:Plasmodium falciparum / Q000201:enzymology / Q000235:genetics
D016282:Aspartic Acid Endopeptidases