Aspartyl proteinase genes from apicomplexan parasites:: evidence for evolution of the gene structure

被引:17
作者
Jean, L
Long, MY
Young, J
Péry, P
Tomley, F
机构
[1] Natl Inst Med Res, Div Parasitol, London NW7 1AA, England
[2] Inst Anim Hlth, Compton Lab, Newbury RG20 7NN, Berks, England
[3] Univ Chicago, Dept Ecol & Evolut, Chicago, IL 60637 USA
[4] INRA, Unite Virol & Immunol Mol, F-78352 Jouy En Josas, France
基金
美国国家科学基金会;
关键词
D O I
10.1016/S1471-4922(01)02030-X
中图分类号
R38 [医学寄生虫学]; Q [生物科学];
学科分类号
07 ; 0710 ; 09 ; 100103 ;
摘要
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.
引用
收藏
页码:491 / 498
页数:8
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