| Author | Silva, Isabel Caetano de Abreu da | |
| Author | Carneiro, Vitor Coutinho | |
| Author | Vicentino, Amanda Roberta Revoredo | |
| Author | Aguilera, Estefania Anahi | |
| Author | Mohana-Borges, Ronaldo | |
| Author | Thiengo, Silvana | |
| Author | Fernandez, Monica Ammon | |
| Author | Fantappié, Marcelo Rosado | |
| Access date | 2016-06-21T14:18:53Z | pt_BR |
| Access date | 2016-07-07T12:25:20Z | |
| Available date | 2016-06-21T14:18:53Z | pt_BR |
| Available date | 2016-07-07T12:25:20Z | |
| Document date | 2016 | |
| Citation | SILVA, Isabel Caetano de Abreu da; et al. The distinct C-terminal acidic domains of HMGB proteins are functionally relevant in Schistosoma mansoni. International Journal for Parasitology, v.46, p.253-262, 2016. | pt_BR |
| ISSN | 0020.7519 | pt_BR |
| URI | https://www.arca.fiocruz.br/handle/icict/14710 | |
| Language | eng | pt_BR |
| Publisher | Elsevier | pt_BR |
| Rights | restricted access | |
| Title | The distinct C-terminal acidic domains of HMGB proteins are functionally relevant in Schistosoma mansoni | pt_BR |
| Type | Article | |
| DOI | 10.1016/j.ijpara.2015.12.007 | pt_BR |
| Abstract | The Schistosoma mansoni High Mobility Group Box (HMGB) proteins SmHMGB1, SmHMGB2 and
SmHMGB3 share highly conserved HMG box DNA binding domains but have significantly different
C-terminal acidic tails. Here, we used three full-length and tailless forms of the S. mansoni HMGB proteins
to examine the functional roles of their acidic tails. DNA binding assays revealed that the different lengths
of the acidic tails among the three SmHMGB proteins significantly and distinctively influenced their DNA
transactions. Spectroscopic analyses indicated that the longest acidic tail of SmHMGB3 contributes to the
structural stabilisation of this protein. Using immunohistochemical analysis, we showed distinct patterns
of SmHMGB1, SmHMGB2 and SmHMGB3 expression in different tissues of adult worms. RNA interference
approaches indicated a role for SmHMGB2 and SmHMGB3 in the reproductive system of female worms,
whereas for SmHMGB1 no clear phenotype was observed. Schistosome HMGB proteins can be phosphorylated,
acetylated and methylated. Importantly, the acetylation and methylation of schistosome HMGBs
were greatly enhanced upon removal of the acidic tail. These data support the notion that the C-terminal
acidic tails dictate the differences in the structure, expression and function of schistosome HMGB
proteins. | pt_BR |
| Affilliation | Universidade Federal do Rio de Janeiro. Instituto de Bioquímica Médica Leopoldo de Meis. Programa de Biologia Molecular e Biotecnologia. Rio de Janeiro, RJ, Brasil. | pt_BR |
| Affilliation | Universidade Federal do Rio de Janeiro. Instituto de Bioquímica Médica Leopoldo de Meis. Programa de Biologia Molecular e Biotecnologia. Rio de Janeiro, RJ, Brasil. | pt_BR |
| Affilliation | Universidade Federal do Rio de Janeiro. Instituto de Bioquímica Médica Leopoldo de Meis. Programa de Biologia Molecular e Biotecnologia. Rio de Janeiro, RJ, Brasil. | pt_BR |
| Affilliation | Universidade Federal do Rio de Janeiro. Instituto de Biofísica Carlos Chagas Filho. Rio de Janeiro, RJ, Brasil. | pt_BR |
| Affilliation | Universidade Federal do Rio de Janeiro. Instituto de Biofísica Carlos Chagas Filho. Rio de Janeiro, RJ, Brasil. | pt_BR |
| Affilliation | Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Malacologia. Rio de Janeiro, RJ, Brasil. | pt_BR |
| Affilliation | Fundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Malacologia. Rio de Janeiro, RJ, Brasil. | pt_BR |
| Affilliation | Universidade Federal do Rio de Janeiro. Instituto de Bioquímica Médica Leopoldo de Meis. Programa de Biologia Molecular e Biotecnologia. Rio de Janeiro, RJ, Brasil. | pt_BR |
| Subject | Schistosoma mansoni | pt_BR |
| Subject | HMGB proteins | pt_BR |
| Subject | DNA binding proteins | pt_BR |
| Subject | DNA transactions | pt_BR |
| DeCS | Proteínas HMGB | pt_BR |
| DeCS | Schistosoma mansoni | pt_BR |
| e-ISSN | 1879-0135 | pt_BR |
