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Conocimientos estructurales y mecanicistas sobre el reconocimiento del tracto poliurídico por el motivo de

Zuzana Cieniková¹, Fred F Damberger, Jonathan Hall

¹Department of Biology, Institute of Molecular Biology and Biophysics, ETH Zürich , 8093 Zürich, Switzerland.

Journal of the American Chemical Society

|September 13, 2014

Resumen

El motivo de reconocimiento de ARN (RRM) de la ribonucleoproteína nuclear heterogénea C (hnRNP C) se une a las secuencias de ARN ricas en uridina. Los estudios estructurales y termodinámicos revelan su mecanismo de unión específico, explicando las interacciones de todo el transcriptoma.

Área de la Ciencia:

Biología Molecular Biología Molecular
Biología Estructural Biología estructural.
La bioquímica es la bioquímica.

Sus antecedentes:

La ribonucleoproteína nuclear heterogénea C (hnRNP C) es un factor regulador clave del ARN en el núcleo.
Se sabe que su motivo de reconocimiento de ARN (RRM) une secuencias ricas en uridina.

Objetivo del estudio:

Para aclarar los detalles moleculares y mecanicistas de las interacciones RRM-ARN.
Para entender cómo hnRNP C se une a los tractos de la uridina a nivel molecular.

Principales métodos:

Se determinaron las estructuras de solución de las RRM complejas con poli (U) oligómeros (5 y 7 nucleótidos).
Un nuevo enfoque computacional integró el consenso de reconocimiento estructural con descripciones vinculantes termodinámicas.

Principales resultados:

El RRM exhibe un gradiente de 5' a 3' de selectividad de la uridina a través de sus cinco bolsillos de unión.
Esta selectividad explica la preferencia por los tractos urinarios contiguos.
Los patrones modelados de unión a proteínas predicen con precisión los datos de enlaces cruzados transcriptómicos experimentales para hnRNP C.

Conclusiones:

Se confirma que el RRM es el dominio primario de unión al ARN del tetramero hnRNP C.
Las perspectivas estructurales proporcionan un marco para interpretar los datos de unión de ARN de alto rendimiento.

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