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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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 |
work_keys_str_mv |
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1807317708222496768 |