title: The distinct C-terminal acidic domains of HMGB proteins are functionally relevant in Schistosoma mansoni.
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.
authors.affiliation: Instituto de Bioquímica Médica Leopoldo de Meis, Programa de Biologia Molecular e Biotecnologia, Universidade Federal do Rio de Janeiro, Brazil.
authors.forename: Isabel Caetano
authors.initials: IC
authors.lastname: de Abreu da Silva
authors.affiliation: Instituto de Bioquímica Médica Leopoldo de Meis, Programa de Biologia Molecular e Biotecnologia, Universidade Federal do Rio de Janeiro, Brazil.
authors.forename: Vitor Coutinho
authors.initials: VC
authors.lastname: Carneiro
authors.affiliation: Instituto de Bioquímica Médica Leopoldo de Meis, Programa de Biologia Molecular e Biotecnologia, Universidade Federal do Rio de Janeiro, Brazil.
authors.forename: Amanda Roberta Revoredo
authors.initials: AR
authors.lastname: Vicentino
authors.affiliation: Instituto de Biofísica Carlos Chagas Filho, Universidade Federal do Rio de Janeiro, Brazil.
authors.forename: Estefania Anahi
authors.initials: EA
authors.lastname: Aguilera
authors.affiliation: Instituto de Biofísica Carlos Chagas Filho, Universidade Federal do Rio de Janeiro, Brazil.
authors.forename: Ronaldo
authors.initials: R
authors.lastname: Mohana-Borges
authors.affiliation: Laboratório de Malacologia, Fundação Oswaldo Cruz, Instituto Oswaldo Cruz, Brazil.
authors.forename: Silvana
authors.initials: S
authors.lastname: Thiengo
authors.affiliation: Laboratório de Malacologia, Fundação Oswaldo Cruz, Instituto Oswaldo Cruz, Brazil.
authors.forename: Monica Ammon
authors.initials: MA
authors.lastname: Fernandez
authors.affiliation: Instituto de Bioquímica Médica Leopoldo de Meis, Programa de Biologia Molecular e Biotecnologia, Universidade Federal do Rio de Janeiro, Brazil. Electronic address: fantappie@bioqmed.ufrj.br.
authors.forename: Marcelo Rosado
authors.initials: MR
authors.lastname: Fantappié
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002942:Circular Dichroism; D018509:DNA, Helminth / Q000378:metabolism; D005260:Female; D024002:HMGB Proteins / Q000737:chemistry* / Q000235:genetics / Q000502:physiology; D007150:Immunohistochemistry; D008297:Male; D009928:Organ Specificity; D054730:Protein Interaction Domains and Motifs / Q000502:physiology; D011499:Protein Processing, Post-Translational / Q000502:physiology; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D034622:RNA Interference; D012550:Schistosoma mansoni / Q000737:chemistry* / Q000235:genetics
chemical_list: D018509:DNA, Helminth; D024002:HMGB Proteins
keywords: DNA binding proteins; DNA transactions; HMGB proteins; Schistosoma mansoni