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Nucleic Acids Research Advance Access published online on December 9, 2008
Nucleic Acids Research, doi:10.1093/nar/gkn979
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© 2008 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Molecular Biology

A novel role for Gemin5 in mRNA translation

Almudena Pacheco, Sonia López de Quinto, Jorge Ramajo, Noemí Fernández and Encarnación Martínez-Salas*

Centro de Biología Molecular Severo Ochoa, CSIC-UAM, Cantoblanco 28049 Madrid, Spain

*To whom correspondence should be addressed. Tel: +34 911 964 619; Fax: +34 911 964 420; Email: emartinez{at}cbm.uam.es

Received September 15, 2008. Revised November 11, 2008. Accepted November 20, 2008.

In eukaryotic cells translation initiation occurs through two alternative mechanisms, a cap-dependent operating in the majority of mRNAs, and a 5'-end-independent driven by internal ribosome entry site (IRES) elements, specific for a subset of mRNAs. IRES elements recruit the translation machinery to an internal position in the mRNA through a mechanism involving the IRES structure and several trans-acting factors. Here, we identified Gemin5 protein bound to the foot-and-mouth disease virus (FMDV) and hepatitis C virus (HCV) IRES using two independent approaches, riboproteomic analysis and immunoprecipitation of photocroslinked factors. Functional analysis performed in Gemin5 shRNA-depleted cells, or in in vitro translation reactions, revealed an unanticipated role of Gemin5 in translation control as a down-regulator of cap-dependent and IRES-driven translation initiation. Consistent with this, pull-down assays showed that Gemin5 forms part of two distinct complexes, a specific IRES-ribonucleoprotein complex and an IRES-independent protein complex containing eIF4E. Thus, beyond its role in snRNPs biogenesis, Gemin5 also functions as a modulator of translation activity.

Present address: Sonia López de Quinto, Cardiff University, School of Biosciences, Biomedical Sciences Building, Museum Avenue, Cardiff CF10 3AX, UK


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