Magnesium-dependent folding of a picornavirus IRES element modulates RNA conformation and eIF4G interaction.

ABSTRACT: Internal ribosome entry site (IRES) elements are high-order RNA structures that promote internal initiation of translation to allow protein synthesis under situations that compromise the general cap-dependent translation mechanism. Picornavirus IRES elements are highly efficient elements with a modular RNA structure organization. Here we investigated the effect of Mg(2+) concentration on the local flexibility and solvent accessibility of the foot-and-mouth disease virus (FMDV) IRES element measured on the basis of selective 2'-hydroxyl acylation analyzed by primer extension (SHAPE) reactivity and hydroxyl radical cleavage. We have found that Mg(2+) concentration affects the organization of discrete IRES regions, mainly the apical region of domain 3, the 10 nt loop of domain 4, and the pyri

SUBMITTER: Lozano G 

PROVIDER: S-EPMC4163634 | biostudies-literature | 2014 Aug

REPOSITORIES: biostudies-literature