On the post-translational modificationa at the C-terminal domain of the major cysteine proteinase (cruzipain) fromTrypanosoma cruzi
- 1 December 1992
- journal article
- Published by Oxford University Press (OUP) in FEMS Microbiology Letters
- Vol. 100 (1-3) , 411-416
- https://doi.org/10.1111/j.1574-6968.1992.tb14070.x
Abstract
Cruzipain, the major cysteine proteinase from Trypanosoma cruzi, has a 130 amino acid-long C-terminal domain, which, although microheterogeneous in SDS-PAGE, has a single N-terminal amino acid sequence. Most of the Thr residues present at the beginning of this sequence are modified; the nature of this modification is still unknown, but O-glycosylation and phosphorylation seem both to be absent. The only potential site for N-glycosylation (Asn 254) is glycosylated in vivo. Most of the eight Cys residues are involved in disulfide bridges. The results are consistent with cruzipain being made of two well-defined domains, a catalytic one with high homology to cathepsin L, and a C-terminal domain, linked to the former by a 'hinge' corresponding to the Pro- and Thr-rich region at its N-terminus.Keywords
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