Título
Molecular Cloning of a cDNA Encoding for Taenia solium TATA-Box Binding Protein 1 (TsTBP1) and Study of Its Interactions with the TATA-Box of Actin 5 and Typical 2-Cys Peroxiredoxin Genes.
Autor
Oscar Rodriguez Lima
Ponciano Garcia Gutierrez
Lucía Jiménez
Angel Alfonso Zarain Herzberg
Roberto Carlos Lazzarini Lechuga
Abraham Landa Piedra
Nivel de Acceso
Acceso Abierto
Identificador alterno
doi: 10.1371/journal.pone.0141818
Materias
Parasitología - ([PLOS ONE (1932-6203) vol. 10(11), 1-17 (2015)]) Taenia solium - ([PLOS ONE (1932-6203) vol. 10(11), 1-17 (2015)]) Factores de transcripción - ([PLOS ONE (1932-6203) vol. 10(11), 1-17 (2015)]) Genómica - ([PLOS ONE (1932-6203) vol. 10(11), 1-17 (2015)]) Producción de anticuerpos - ([PLOS ONE (1932-6203) vol. 10(11), 1-17 (2015)]) Proteomica - ([PLOS ONE (1932-6203) vol. 10(11), 1-17 (2015)]) BIOLOGÍA Y QUÍMICA - (CTI)
Resumen o descripción
TATA-box binding protein (TBP) is an essential regulatory transcription factor for the TATA-box and TATA-box-less gene promoters. We report the cloning and characterization of a full-length cDNA that encodes a Taenia solium TATA-box binding protein 1 (TsTBP1). Deduced amino acid composition from its nucleotide sequence revealed that encodes a protein of 238 residues with a predicted molecular weight of 26.7 kDa, and a theoretical pI of 10.6. The NH2-terminal domain shows no conservation when compared with to pig and human TBP1s. However, it shows high conservation in size and amino acid identity with taeniids TBP1s. In contrast, the TsTBP1 COOH-terminal domain is highly conserved among organisms, and contains the amino acids involved in interactions with the TATA-box, as well as with TFIIA and TFIIB. In silico TsTBP1 modeling reveals that the COOH-terminal domain forms the classical saddle structure of the TBP family, with one ?-helix at the end, not present in pig and human. Native TsTBP1 was detected in T. solium cysticerci´s nuclear extract by western blot using rabbit antibodies generated against two synthetic peptides located in the NH2 and COOH-terminal domains of TsTBP1. These antibodies, through immunofluorescence technique, identified the TBP1 in the nucleus of cells that form the bladder wall of cysticerci of Taenia crassiceps, an organism close related to T. solium. Electrophoretic mobility shift assays using nuclear extracts from T. solium cysticerci and antibodies against the NH2-terminal domain of TsTBP1 showed the interaction of native TsTBP1 with the TATA-box present in T. solium actin 5 (pAT5) and 2-Cys peroxiredoxin (Ts2-CysPrx) gene promoters; in contrast, when antibodies against the anti-COOH-terminal domain of TsTBP1 were used, they inhibited the binding of TsTBP1 to the TATA-box of the pAT5 promoter gene.
Editor
Public Library of Science
Fecha de publicación
2015
Tipo de publicación
Artículo
Versión de la publicación
Versión publicada
Recurso de información
Formato
application/pdf
Fuente
PLOS ONE (1932-6203) vol. 10(11), 1-17 (2015)
Idioma
Inglés
Relación
https://www.ncbi.nlm.nih.gov/pmc/issues/260222/
Cobertura
US
Repositorio Orígen
Repositorio Institucional de la Facultad de Medicina,UNAM.Departamento de Microbiologia y Parasitologia
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