Digital.CSIC > Biología y Biomedicina > Centro de Biología Molecular Severo Ochoa (CBM) > (CBM) Artículos >




Open Access item Differential cleavage of eIF4GI and eIF4GII in mammalian cells. Effects on translation

Authors:Castelló, Alfredo
Alvarez, Enrique
Carrasco Llamas, Luis
Keywords:Vaccinia virus T7, Encephalomyocarditis virus
Issue Date:7-Sep-2006
Publisher:American Society for Biochemistry and Molecular Biology
Citation:Journal of Biological Chemistry 281(44): 33206-33216 (2006)
Abstract:Two isoforms of the translation initiation factor eIF4G, eIF4GI and eIF4GII, have been described in eukaryotic cells. The exact function of each isoform during the initiation of protein synthesis is still under investigation. We have developed an efficient and reliable method of expressing poliovirus 2Apro, which differentially proteolyzes eIF4GI and eIF4GII in a time- and dose-dependent manner. This system is based on the electroporation of an in vitro transcribed mRNA that contains the encephalomyocarditis virus internal ribosome entry site followed by the sequence of poliovirus 2Apro. In contrast to HeLa cells, expression of this protease in BHK-21 cells induces delayed hydrolysis kinetics of eIF4GI with respect to eIF4GII. Moreover, under these conditions the polyadenylate binding protein is not cleaved. Interestingly, translation of de novo synthesized luciferase mRNA is highly dependent on eIF4GI integrity, whereas ongoing translation is inhibited at the same time as eIF4GII cleavage. Moreover, reinitiation of a preexisting mRNA translation after polysome run-off is dependent on the integrity of eIF4GII. Notably, de novo translation of heat shock protein 70 mRNA depends little on eIF4GI integrity but is more susceptible to eIF4GII hydrolysis. Finally, translation of an mRNA containing encephalomyocarditis virus internal ribosome entry site when the two isoforms of eIF4G are differentially hydrolyzed has been examined
Description:El pdf del artículo es la versión post-print.-- Article available at http://www.jbc.org/cgi/content/abstract/M604340200v1
Publisher version (URL):http://dx.doi.org/10.1074/jbc.M604340200
E-ISSNmetadata.dc.identifier.doi = DOI:1083-351X
Appears in Collections:(CNB) Artículos
(CBM) Artículos

Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.