HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS		QUICK SEARCH:   [advanced] Author: Keyword(s): Year:  Vol:  Page:

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Bassili, G. Articles by Niepmann, M. Search for Related Content PubMed PubMed Citation Articles by Bassili, G. Articles by Niepmann, M. Agricola Articles by Bassili, G. Articles by Niepmann, M.

Sequence and secondary structure requirements in a highly conserved element for foot-and-mouth disease virus internal ribosome entry site activity and eIF4G binding

Lanja Saleh

Kerstin Ochs

Institute of Biochemistry, Faculty of Medicine, Friedrichstrasse 24, 35392 Giessen, Germany

Correspondence
Michael Niepmann
michael.niepmann{at}biochemie.med.uni-giessen.de

Foot-and-mouth disease virus (FMDV) and other picornaviruses initiate translation of their positive-strand RNA genomes at the highly structured internal ribosome entry site (IRES), which mediates ribosome recruitment to an internal site of the virus RNA. This process is facilitated by eukaryotic translation initiation factors (eIFs), such as eIF4G and eIF4B. In the eIF4G-binding site, a characteristic, discontinuous sequence element is highly conserved within the cardio- and aphthovirus subgroup (including FMDV) of the picornaviruses. This conserved element was mutated in order to investigate its primary sequence and secondary structure requirements for IRES function. Both binding of eIF4G to the IRES and IRES-directed translation are seriously impaired by mutations in two unpaired dinucleotide stretches that are exposed from the double-stranded (ds)RNA. In the base-paired regions of the conserved element, maintenance of the double-stranded secondary structure is essential, whilst in some cases, the primary sequence within the dsRNA regions is also important for IRES function. Extra eIF4F added to the translation reaction does not restore full IRES activity or eIF4G binding, indicating that disturbances in the structure of this conserved element cannot be overcome by increased initiation factor concentrations.

Present address: Friedrich-Miescher Institute, 4058 Basel, Switzerland.

Present address: EISAI GmbH, Lyoner Strasse 14, D-60528 Frankfurt, Germany.

This article has been cited by other articles:

				O. Fernandez-Miragall and E. Martinez-Salas In vivo footprint of a picornavirus internal ribosome entry site reveals differences in accessibility to specific RNA structural elements J. Gen. Virol., November 1, 2007; 88(11): 3053 - 3062. [Abstract] [Full Text] [PDF]

				C. Junemann, Y. Song, G. Bassili, D. Goergen, J. Henke, and M. Niepmann Picornavirus Internal Ribosome Entry Site Elements Can Stimulate Translation of Upstream Genes J. Biol. Chem., January 5, 2007; 282(1): 132 - 141. [Abstract] [Full Text] [PDF]

				Y. SONG, E. TZIMA, K. OCHS, G. BASSILI, H. TRUSHEIM, M. LINDER, K. T. PREISSNER, and M. NIEPMANN Evidence for an RNA chaperone function of polypyrimidine tract-binding protein in picornavirus translation RNA, December 1, 2005; 11(12): 1809 - 1824. [Abstract] [Full Text] [PDF]