RNA-Binding Proteins Revisited – The Emerging Arabidopsis mRNA Interactome. (June 2017)

• Record Type: Journal Article
• Authors: Köster, Tino; Marondedze, Claudius; Meyer, Katja; Staiger, Dorothee
• Is Part Of: Trends in plant science. Volume 22:Number 6(2017)
• Page Start: 512
• Page End: 526
• Publication Date: 2017-06
• Subjects: RNA-binding protein -- mRNA interactome -- UV crosslinking -- mRNP particles; Botany -- Periodicals; Botanique -- Périodiques; Botany; Periodicals; 580.5
• DOI: 10.1016/j.tplants.2017.03.009
• Languages: English
• ISSNs: 1360-1385

Abstract

Abstract : RNA–protein interaction is an important checkpoint to tune gene expression at the RNA level. Global identification of proteins binding in vivo to mRNA has been possible through interactome capture – where proteins are fixed to target RNAs by UV crosslinking and purified through affinity capture of polyadenylated RNA. In arabidopsis over 500 RNA-binding proteins (RBPs) enriched in UV-crosslinked samples have been identified. As in mammals and yeast, the mRNA interactomes came with a few surprises. For example, a plethora of the proteins caught on RNA had not previously been linked to RNA-mediated processes, for example proteins of intermediary metabolism. Thus, the studies provide unprecedented insights into the composition of the mRNA interactome, highlighting the complexity of RNA-mediated processes. Trends: UV crosslinking in vivo combined with oligo(dT) affinity purification of poly(A) + RNAs allows the identification of mRNA interactomes. Interactome capture is widely applicable to model organisms. Interactome capture in arabidopsis provides experimental evidence of in vivo RNA binding for many candidate RBPs predicted in silico . Proteins not previously known to have a role in RNA-related processes are prominent among mRNA-interacting proteins. Proteins with a role in central metabolism appear in the mRNA interactomes. This may indicate a degree of contamination in the affinity capture of RNA–protein complexes. Proteins identified in more than one interactome could also have functional significance. Independent confirmation of the RNA-binding activity would then point to a double-life of metabolic enzymes in RNA biology.