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Artículo

The FIP-1 like polyadenylation factor in trypanosomes and the structural basis for its interaction with CPSF30

Bercovich, NataliaIcon ; Levin, Mariano JorgeIcon ; Vazquez, Martin PabloIcon
Fecha de publicación: 03/2009
Editorial: Academic Press Inc Elsevier Science
Revista: Biochemical and Biophysical Research Communications
ISSN: 0006-291X
Idioma: Inglés
Tipo de recurso: Artículo publicado
Clasificación temática:
Biología Celular, Microbiología

Resumen

In trypanosomes transcription is polycistronic and individual mRNAs are generated by a trans-splicing/polyadenylation coupled reaction. We identified a divergent trypanosome FIP1-like, a factor required for mRNA 3′ end formation from yeasts to human. Here we showed that it is a nuclear protein with a speckled distribution essential for trypanosome viability. A strong interaction was found between TcFIP1-like and TcCPSF30, a component of the polyadenylation complex. We determined the specific amino acids in each protein involved in the interaction. Significant differences were found between the trypanosome interaction surface and its human counterpart. Although CPSF30/FIP1 interaction is known in other organisms, this is the first report mapping the interaction surface at the amino acid level.
Palabras clave: Drug Target , Mrna Processing , Polyadenylation Factors , Protein Interactions , Trypanosome Diseases
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info:eu-repo/semantics/openAccess Excepto donde se diga explícitamente, este item se publica bajo la siguiente descripción: Creative Commons Attribution-NonCommercial-ShareAlike 2.5 Unported (CC BY-NC-SA 2.5)
Identificadores
URI: http://hdl.handle.net/11336/79488
URL: https://www.ncbi.nlm.nih.gov/pubmed/19338765
URL: https://doi.org/10.1016/j.bbrc.2009.01.182
Colecciones
Articulos(INGEBI)
Articulos de INST.DE INVEST.EN ING.GENETICA Y BIOL.MOLECULAR "DR. HECTOR N TORRES"
Citación
Bercovich, Natalia; Levin, Mariano Jorge; Vazquez, Martin Pablo; The FIP-1 like polyadenylation factor in trypanosomes and the structural basis for its interaction with CPSF30; Academic Press Inc Elsevier Science; Biochemical and Biophysical Research Communications; 380; 4; 3-2009; 850-855
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