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A cysteine proteinase cDNA from Trypanosoma brucei predicts an enzyme with an unusual C‐terminal extension
Author(s) -
Mottram Jeremy C.,
North Michael J.,
Barry J.David,
Coombs Graham H.
Publication year - 1989
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(89)81655-2
Subject(s) - trypanosoma brucei , complementary dna , cysteine , biology , biochemistry , enzyme , cathepsin l , cathepsin , homology (biology) , microbiology and biotechnology , peptide sequence , amino acid , gene
A cDNA for a Trypanosoma brucei cysteine proteinase has been cloned and sequenced. The deduced protein can be divided into four domains, based on homologies with other cysteine proteinases: the pre‐, pro‐ and central regions show considerable homology to the cathepsin L class of mammalian enzymes, whilst the long C‐terminal extension distinguishes the trypanosome enzyme from all mammalian cysteine proteinases reported. This 108 amino acid extension, which includes 9 contiguous prolines near the junction with the central domain, appears likely to be processed in part to produce the mature enzyme, and may be involved in targetting the protein within the cell. The trypanosome genome contains more than 20 copies of the cysteine proteinase gene arranged in a long tandem array.