On the post-translational modificationa 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 th...

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Autores principales: Cazzulo, J.J., Martínez, J., Parodi, A.J.A., Wernstedt, C., Hellman, U.
Formato: JOUR
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Acceso en línea:http://hdl.handle.net/20.500.12110/paper_03781097_v100_n1-3_p411_Cazzulo
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spelling todo:paper_03781097_v100_n1-3_p411_Cazzulo2023-10-03T15:31:37Z On the post-translational modificationa at the C-terminal domain of the major cysteine proteinase (cruzipain) from Trypanosoma cruzi Cazzulo, J.J. Martínez, J. Parodi, A.J.A. Wernstedt, C. Hellman, U. Cruzipain Cysteine proteinase Posttranslational modification Proteinase Trypanosoma cruzi cruzipain cysteine proteinase proteinase cruzipain cysteine proteinase peptide fragment article nonhuman priority journal protein processing trypanosoma cruzi amino acid sequence animal genetics isolation and purification metabolism molecular genetics protein processing Trypanosoma cruzi Amino Acid Sequence Animal Cysteine Endopeptidases Molecular Sequence Data Peptide Fragments Protein Processing, Post-Translational Support, Non-U.S. Gov't 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. © 1992. Fil:Martínez, J. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. Fil:Parodi, A.J.A. Universidad de Buenos Aires. Facultad de Ciencias Exactas y Naturales; Argentina. JOUR info:eu-repo/semantics/openAccess http://creativecommons.org/licenses/by/2.5/ar http://hdl.handle.net/20.500.12110/paper_03781097_v100_n1-3_p411_Cazzulo
institution Universidad de Buenos Aires
institution_str I-28
repository_str R-134
collection Biblioteca Digital - Facultad de Ciencias Exactas y Naturales (UBA)
topic Cruzipain
Cysteine proteinase
Posttranslational modification
Proteinase
Trypanosoma cruzi
cruzipain
cysteine proteinase
proteinase
cruzipain
cysteine proteinase
peptide fragment
article
nonhuman
priority journal
protein processing
trypanosoma cruzi
amino acid sequence
animal
genetics
isolation and purification
metabolism
molecular genetics
protein processing
Trypanosoma cruzi
Amino Acid Sequence
Animal
Cysteine Endopeptidases
Molecular Sequence Data
Peptide Fragments
Protein Processing, Post-Translational
Support, Non-U.S. Gov't
Trypanosoma cruzi
spellingShingle Cruzipain
Cysteine proteinase
Posttranslational modification
Proteinase
Trypanosoma cruzi
cruzipain
cysteine proteinase
proteinase
cruzipain
cysteine proteinase
peptide fragment
article
nonhuman
priority journal
protein processing
trypanosoma cruzi
amino acid sequence
animal
genetics
isolation and purification
metabolism
molecular genetics
protein processing
Trypanosoma cruzi
Amino Acid Sequence
Animal
Cysteine Endopeptidases
Molecular Sequence Data
Peptide Fragments
Protein Processing, Post-Translational
Support, Non-U.S. Gov't
Trypanosoma cruzi
Cazzulo, J.J.
Martínez, J.
Parodi, A.J.A.
Wernstedt, C.
Hellman, U.
On the post-translational modificationa at the C-terminal domain of the major cysteine proteinase (cruzipain) from Trypanosoma cruzi
topic_facet Cruzipain
Cysteine proteinase
Posttranslational modification
Proteinase
Trypanosoma cruzi
cruzipain
cysteine proteinase
proteinase
cruzipain
cysteine proteinase
peptide fragment
article
nonhuman
priority journal
protein processing
trypanosoma cruzi
amino acid sequence
animal
genetics
isolation and purification
metabolism
molecular genetics
protein processing
Trypanosoma cruzi
Amino Acid Sequence
Animal
Cysteine Endopeptidases
Molecular Sequence Data
Peptide Fragments
Protein Processing, Post-Translational
Support, Non-U.S. Gov't
Trypanosoma cruzi
description 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. © 1992.
format JOUR
author Cazzulo, J.J.
Martínez, J.
Parodi, A.J.A.
Wernstedt, C.
Hellman, U.
author_facet Cazzulo, J.J.
Martínez, J.
Parodi, A.J.A.
Wernstedt, C.
Hellman, U.
author_sort Cazzulo, J.J.
title On the post-translational modificationa at the C-terminal domain of the major cysteine proteinase (cruzipain) from Trypanosoma cruzi
title_short On the post-translational modificationa at the C-terminal domain of the major cysteine proteinase (cruzipain) from Trypanosoma cruzi
title_full On the post-translational modificationa at the C-terminal domain of the major cysteine proteinase (cruzipain) from Trypanosoma cruzi
title_fullStr On the post-translational modificationa at the C-terminal domain of the major cysteine proteinase (cruzipain) from Trypanosoma cruzi
title_full_unstemmed On the post-translational modificationa at the C-terminal domain of the major cysteine proteinase (cruzipain) from Trypanosoma cruzi
title_sort on the post-translational modificationa at the c-terminal domain of the major cysteine proteinase (cruzipain) from trypanosoma cruzi
url http://hdl.handle.net/20.500.12110/paper_03781097_v100_n1-3_p411_Cazzulo
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