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The C-terminal RNA binding motif of HuR is a multi-functional domain leading to HuR oligomerization and binding to U-rich RNA targets

Opened Access The C-terminal RNA binding motif of HuR is a multi-functional domain leading to HuR oligomerization and binding to U-rich RNA targets

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Autor: Scheiba, Rafael M.
Ibáñez de Okapua, Alain
Díaz Quintana, Antonio Jesús
Cruz Gallardo, Isabel
Martínez Cruz, Luis Alfonso
Martínez Chantar, María L.
Blanco, Francisco J.
Díaz Moreno, Irene
Departamento: Universidad de Sevilla. Departamento de Bioquímica Vegetal y Biología Molecular
Fecha: 2014
Publicado en: RNA Biology, 11 (10), 1250-1261.
Tipo de documento: Artículo
Resumen: Human antigen R (HuR) is a 32 kDa protein with 3 RNA Recognition Motifs (RRMs), which bind to Adenylate and uridylate Rich Elements (AREs) of mRNAs. Whereas the N-terminal and central domains (RRM1 and RRM2) are essential for AREs recognition, little is known on the C-terminal RRM3 beyond its implication in HuR oligomerization and apoptotic signaling. We have developed a detergent-based strategy to produce soluble RRM3 for structural studies. We have found that it adopts the typical RRM fold, does not interact with the RRM1 and RRM2 modules, and forms dimers in solution. Our NMR measurements, combined with Molecular Dynamics simulations and Analytical Ultracentrifugation experiments, show that the protein dimerizes through a helical region that contains the conserved W261 residue. We found that HuR RRM3 binds to 5'-mer U-rich RNA stretches through the solvent exposed side of its β-sheet, located opposite to the dimerization site. Upon mimicking phosphorylation by the S318D replacement...
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Cita: Scheiba, R.M., Ibáñez de Okapua, A., Díaz Quintana, A., Cruz Gallardo, I., Martínez Cruz, L.A., Martínez Chantar, M.L.,...,Díaz Moreno, I. (2014). The C-terminal RNA binding motif of HuR is a multi-functional domain leading to HuR oligomerization and binding to U-rich RNA targets. RNA Biology, 11 (10), 1250-1261.
Tamaño: 1.678Mb
Formato: PDF

URI: https://hdl.handle.net/11441/69276

DOI: 10.1080/15476286.2014.996069

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