Primary structure and partial characterization of a life-cycle-regulated cysteine protease from Trypanosoma (Nannomonas) congolense.
Trypanosoma (Nannomonas) congolense is an important pathogenic parasite of domestic livestock in Africa. We have cloned a cDNA encoding a prepro-cysteine protease of this protozoan, the sequence of which indicates it is an early mRNA processing intermediate. Northern analysis demonstrates a life-cycle-stage specificity similar to previously described enzymatic data. The deduced amino-acid sequence shows extensive similarity to cysteine proteases of other parasitic protozoa, as well as papain and cathepsin L. As with other African trypanosomes, a poly-proline tract connects the catalytic domain with an unusual C-terminal extension.
Fish
W R
WR
International Laboratory for Research on Animal Diseases (ILRAD), Nairobi, Kenya.
Nkhungulu
Z M
ZM
Muriuki
C W
CW
Ndegwa
D M
DM
Lonsdale-Eccles
J D
JD
Steyaert
J
J
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D015152:Blotting, Northern; D003001:Cloning, Molecular; D003546:Cysteine Endopeptidases / Q000737:chemistry / Q000235:genetics*; D018076:DNA, Complementary; D015971:Gene Expression Regulation, Enzymologic; D008969:Molecular Sequence Data; D014348:Trypanosoma congolense / Q000201:enzymology* / Q000235:genetics / Q000254:growth & development
D018076:DNA, Complementary; D003546:Cysteine Endopeptidases