Papel de la proteína similar a la ubiquitina Hub1 en el uso en el sitio de empalme y en el empalme alternativo

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Shravan Kumar Mishra¹, Tim Ammon, Grzegorz M Popowicz

¹Department of Molecular Cell Biology, Max Planck Institute of Biochemistry, Am Klopferspitz 18, 82152 Martinsried, Germany.

|May 27, 2011

Resumen

La proteína similar a la ubiquitina Hub1 promueve el empalme alternativo al unirse a los espliceosomas. Esta interacción es crucial para reconocer sitios específicos de empalme, lo que permite la diversidad de productos genéticos.

Área de la Ciencia:

Biología Molecular Biología Molecular
Genética La genética.
La bioquímica es la bioquímica.

Sus antecedentes:

El empalme alternativo diversifica los productos genéticos de los eucariotas.
El reconocimiento de sitios de empalme mediado por spliceosome es esencial para el procesamiento preciso de ARN.

Objetivo del estudio:

Para investigar el papel de la proteína similar a la ubiquitina Hub1 en el empalme alternativo.
Para dilucidar el mecanismo por el cual Hub1 influye en la selección del sitio de empalme.

Principales métodos:

Análisis estructurales y bioquímicos de las interacciones Hub1-spliceosome.
Estudios genéticos utilizando Saccharomyces cerevisiae para evaluar los defectos de empalme en los mutantes con deficiencia de Hub1.

Principales resultados:

Hub1 se une no covalentemente al elemento HIND en las proteínas espliceosomales.
Hub1 facilita el uso de sitios de empalme de 5' no canónicos, promoviendo el empalme SRC1 alternativo.
La pérdida de Hub1 o una interacción defectuosa de Hub1-HIND perjudica el empalme alternativo.

Conclusiones:

Hub1 actúa como un nuevo regulador de empalme alternativo mediante la modificación de la función del espliceosoma.
La modificación no covalente del espliceosoma por proteínas similares a la ubiquitina es un mecanismo clave para la utilización del sitio de empalme.

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