Author | Galetovic, Alexandra | |
Author | Souza, Renata Torres de | |
Author | Santos, Marcia R. M. | |
Author | Cordero-Veas, Esteban Mauricio | |
Author | Bastos, Izabela Marques Dourado | |
Author | Santana, Jaime Martins de | |
Author | Ruiz, Jerônimo Conceição | |
Author | Lima, Fabio Mitsuo | |
Author | Mortara, Renato Arruda | |
Author | Silveira, José Franco da | |
Access date | 2014-10-29T18:07:05Z | |
Available date | 2014-10-29T18:07:05Z | |
Document date | 2011 | |
Citation | GALETOVIC, Alexandra et al. The Repetitive Cytoskeletal Protein H49 of Trypanosoma cruzi Is a Calpain-Like Protein Located at the Flagellum Attachment Zone. PLoS One 6(11): -e27634, 2011 | pt_BR |
ISSN | 1932-6203 | |
ISSN | 10.1371/journal.pone.0027634 | |
URI | https://www.arca.fiocruz.br/handle/icict/8693 | |
Language | eng | pt_BR |
Publisher | Public Library of Science | pt_BR |
Rights | open access | pt_BR |
Title | The Repetitive Cytoskeletal Protein H49 of Trypanosoma cruzi Is a Calpain-Like Protein Located at the Flagellum Attachment Zone. PLoS One 6(11): -e27634, 2011 | pt_BR |
Type | Article | pt_BR |
Abstract | Sequence alignment Sequence databases Background: Trypanosoma cruzi has a single flagellum attached to the cell body by a network of specialized cytoskeletal and membranous connections called the flagellum attachment zone. Previously, we isolated a DNA fragment (clone H49) which encodes tandemly arranged repeats of 68 amino acids associated with a high molecular weight cytoskeletal protein. In the current study, the genomic complexity of H49 and its relationships to the T. cruzi calpain-like cysteine peptidase family, comprising active calpains and calpain-like proteins, is addressed. Immunofluorescence analysis and biochemical fractionation were used to demonstrate the cellular location of H49 proteins.
Methods and Findings: All of H49 repeats are associated with calpain-like sequences. Sequence analysis demonstrated that this protein, now termed H49/calpain, consists of an amino-terminal catalytic cysteine protease domain II, followed by a large region of 68-amino acid repeats tandemly arranged and a carboxy-terminal segment carrying the protease domains II and III. The H49/calpains can be classified as calpain-like proteins as the cysteine protease catalytic triad has been partially conserved in these proteins. The H49/calpains repeats share less than 60% identity with other calpain-like proteins in Leishmania and T. brucei, and there is no immunological cross reaction among them. It is suggested that the expansion of H49/calpain repeats only occurred in T. cruzi after separation of a T. cruzi ancestor from other trypanosomatid lineages. Immunofluorescence and immunoblotting experiments demonstrated that H49/calpain is located along the flagellum attachment zone adjacent to the cell body.
Conclusions: H49/calpain contains large central region composed of 68-amino acid repeats tandemly arranged. They can be classified as calpain-like proteins as the cysteine protease catalytic triad is partially conserved in these proteins. H49/calpains could have a structural role, namely that of ensuring that the cell body remains attached to the flagellum by connecting the subpellicular microtubule array to it. | pt_BR |
Affilliation | Universidade Federal de São Paulo. Escola Paulista de Medicina. Departamento de Microbiologia, Imunologia e Parasitologia. São Paulo, SP, Brasil/Universidad de Antofagasta. Departamento Biomédico. Laboratório de Bioquímica. Antofagasta, Chile | pt_BR |
Affilliation | Universidade Federal de São Paulo. Escola Paulista de Medicina. Departamento de Microbiologia, Imunologia e Parasitologia. São Paulo, SP, Brasil | pt_BR |
Affilliation | Universidade Bandeirante. São Paulo, SP, Brasil | pt_BR |
Affilliation | Universidade Federal de São Paulo. Escola Paulista de Medicina. Departamento de Microbiologia, Imunologia e Parasitologia. São Paulo, SP, Brasil | pt_BR |
Affilliation | Universidade de Brasília. Instituto de Biologia. Departamento de Biologia Celular. Brasilía, DF, Brasil | pt_BR |
Affilliation | Universidade de Brasília. Instituto de Biologia. Departamento de Biologia Celular. Brasilía, DF, Brasil | pt_BR |
Affilliation | Fundação Oswaldo Cruz. Centro de Pesquisa René Rachou. Belo Horizonte, MG, Brasil | pt_BR |
Affilliation | Universidade Federal de São Paulo. Escola Paulista de Medicina. Departamento de Microbiologia, Imunologia e Parasitologia. São Paulo, SP, Brasil | pt_BR |
Affilliation | Universidade Federal de São Paulo. Escola Paulista de Medicina. Departamento de Microbiologia, Imunologia e Parasitologia. São Paulo, SP, Brasil | pt_BR |
Affilliation | Universidade Federal de São Paulo. Escola Paulista de Medicina. Departamento de Microbiologia, Imunologia e Parasitologia. São Paulo, SP, Brasil | pt_BR |
Affilliation | Universidade Federal de São Paulo. Escola Paulista de Medicina. Departamento de Microbiologia, Imunologia e Parasitologia. São Paulo, SP, Brasil | pt_BR |
Subject | Cytoskeleton | pt_BR |
Subject | Epimastigotes | pt_BR |
Subject | Genomic databases | pt_BR |
Subject | Membrane proteins | pt_BR |
Subject | Proteases | pt_BR |
Subject | Trypanosoma cruzi | pt_BR |