On the post-translational modifications at the C-terminal domain of the major cysteine proteinase (cruzipain) from Trypanosoma cruzi.
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.
Cazzulo
J J
JJ
Instituto de Investigaciones Bioquímicas Luis F. Leloir, Fundación Campomar-CONICET-Facultad de Ciencias Exactas y Naturales, Universidad de Buenos Aires, Argentina.
Martínez
J
J
Parodi
A J
AJ
Wernstedt
C
C
Hellman
U
U
D000595:Amino Acid Sequence; D000818:Animals; D003546:Cysteine Endopeptidases / Q000235:genetics / Q000378:metabolism*; D008969:Molecular Sequence Data; D010446:Peptide Fragments / Q000235:genetics / Q000302:isolation & purification; D011499:Protein Processing, Post-Translational; D015800:Protozoan Proteins; D014349:Trypanosoma cruzi / Q000235:genetics / Q000378:metabolism*
D010446:Peptide Fragments; D015800:Protozoan Proteins; D003546:Cysteine Endopeptidases; C063214:cruzipain