Primary structure and partial characterization of a life-cycle-regulated cysteine protease from Trypanosoma (Nannomonas) congolense.

TitlePrimary structure and partial characterization of a life-cycle-regulated cysteine protease from Trypanosoma (Nannomonas) congolense.
Publication TypeJournal Article
Year of Publication1995
AuthorsFish, W. R., Z. M. Nkhungulu, C. W. Muriuki, D. M. Ndegwa, J. D. Lonsdale-Eccles, and J. Steyaert
JournalGene
Volume161
Issue1
Pagination125-8
Date Published1995 Aug 8
ISSN0378-1119
KeywordsAmino Acid Sequence, Animals, Base Sequence, Blotting, Northern, Cloning, Molecular, Cysteine Endopeptidases, DNA, Complementary, Gene Expression Regulation, Enzymologic, Molecular Sequence Data, Trypanosoma congolense
Abstract

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.

Alternate JournalGene
PubMed ID7642126