Trading translation with RNA-binding proteins

Abstract

RNA-binding proteins regulate every aspect of RNA metabolism, including pre-mRNA splicing, mRNA trafficking, stability, and translation. This review summarizes the available information on molecular mechanisms of translational repression by RNAbinding proteins. By using a specific set of well-defined examples, we also describe how regulation can be reversed.

Translation and replication of hepatitis C virus genomic RNA depends on ancient cellular proteins that control mRNA fates

“…This may be explained by an effect solely at the translation level or by an independent effect on both translation and replication as observed in the BMV model. Such an apparently antagonistic function, to promote both translation and exit from translation, is not without precedent as cellular proteins acting in 2 antagonistic processes such as translation initiation and translation repression have been described (23). An advantage of using a single complex for opposing outcomes seems to be the possibility of responding rapidly to different cellular requirements.…”

Cytoplasmic polyadenylation and translational control

“…mRNA-bound eIF4G recruits the 43S ribosomal complex via contacts with eIF3. Many translational control mechanisms modulate these early steps of translation initiation, and cytoplasmic polyadenylation is not an exception [4,5].…”

On nucleotide solvent accessibility in RNA structure

“…RNAlocated functional sites form steric conformations specifically adapted for interaction with a corresponding protein or with other molecules. This conformation is provided by certain combinations of nucleotides (either in the linear form or as a part of the RNA secondary structuree.g., Iron Responsive Element (Volz, 2008) (for review, see (Abaza and Gebauer, 2008;Sonenberg and Hinnebasch, 2009;Van Der Kelen et al, 2009)). In most cases the nucleotides in positions of the proteinbinding site differ in their functional importance-mutations in some positions abolish binding whereas mutations in other positions are either neutral or influence the functional activity quantitatively (Chatterjee and Pal, 2009).…”