A cysteine proteinase cDNA from Trypanosoma brucei predicts an enzyme with an unusual C-terminal extension.
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 targeting the protein within the cell. The trypanosome genome contains more than 20 copies of the cysteine proteinase gene arranged in a long tandem array.
Mottram
J C
JC
Wellcome Unit of Molecular Parasitology, University of Glasgow, Scotland.
North
M J
MJ
Barry
J D
JD
Coombs
G H
GH
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D015139:Blotting, Southern; D003546:Cysteine Endopeptidases / Q000235:genetics*; D004247:DNA / Q000235:genetics* / Q000302:isolation & purification; D005796:Genes; D008969:Molecular Sequence Data; D008970:Molecular Weight; D015345:Oligonucleotide Probes; D012689:Sequence Homology, Nucleic Acid; D014346:Trypanosoma brucei brucei / Q000201:enzymology / Q000235:genetics*
D015345:Oligonucleotide Probes; D004247:DNA; D003546:Cysteine Endopeptidases