dc.creatorGaletovic, Alexandra
dc.creatorSouza, Renata Torres de
dc.creatorSantos, Marcia R. M.
dc.creatorCordero-Veas, Esteban Mauricio
dc.creatorBastos, Izabela Marques Dourado
dc.creatorSantana, Jaime Martins de
dc.creatorRuiz, Jerônimo Conceição
dc.creatorLima, Fabio Mitsuo
dc.creatorMortara, Renato Arruda
dc.creatorSilveira, José Franco da
dc.date2014-10-29T18:07:05Z
dc.date2014-10-29T18:07:05Z
dc.date2011
dc.date.accessioned2023-09-26T20:31:49Z
dc.date.available2023-09-26T20:31:49Z
dc.identifierGALETOVIC, 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
dc.identifier1932-6203
dc.identifier10.1371/journal.pone.0027634
dc.identifierhttps://www.arca.fiocruz.br/handle/icict/8693
dc.identifier.urihttps://repositorioslatinoamericanos.uchile.cl/handle/2250/8858912
dc.descriptionSequence 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.
dc.formatapplication/pdf
dc.languageeng
dc.publisherPublic Library of Science
dc.rightsopen access
dc.subjectCytoskeleton
dc.subjectEpimastigotes
dc.subjectGenomic databases
dc.subjectMembrane proteins
dc.subjectProteases
dc.subjectTrypanosoma cruzi
dc.titleThe Repetitive Cytoskeletal Protein H49 of Trypanosoma cruzi Is a Calpain-Like Protein Located at the Flagellum Attachment Zone. PLoS One 6(11): -e27634, 2011
dc.typeArticle


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