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

Publication Type:

Journal Article

Authors:

Fish,W.R.; Nkhungulu,Z.M.; Muriuki,C.W.; Ndegwa,D.M.; Lonsdale-Eccles,J.D.; Steyaert,J.

Source:

Volume 161, Issue 1, p.125 - 128 (1995)

URL:

PM:7642126

Keywords:

Amino Acid Sequence; analysis; Animals; Base Sequence; Blotting; Northern; Catalytic Domain; chemistry; Cloning; Molecular; Cysteine Endopeptidases; DNA; DNA; Complementary; DOMAIN; enzymology; Gene Expression Regulation; Enzymologic; genetics; growth & devel

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

Notes:

DA - 19950921
IS - 0378-1119 (Print)
LA - eng
PT - Journal Article
RN - 0 (DNA, Complementary)
RN - EC 3.4.22.- (Cysteine Endopeptidases)
SB - IM