Journal
NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 22, Issue 12, Pages 1027-1033Publisher
NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb.3128
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Funding
- 'Sinergia' grant from the Swiss National Science Foundation [CSRII3-141942]
- Biotechnology and Biological Sciences Research Council [BB1K009303/1]
- Biotechnology and Biological Sciences Research Council [BB/K009303/1] Funding Source: researchfish
- BBSRC [BB/K009303/1] Funding Source: UKRI
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RNA-binding proteins (RBPs) are essential for post-transcriptional regulation of gene expression. Recent high-throughput screens have dramatically increased the number of experimentally identified RBPs; however, comprehensive identification of RBPs within living organisms is elusive. Here we describe the repertoire of 765 and 594 proteins that reproducibly interact with polyadenylated mRNAs in Saccharomyces cerevisiae and Caenorhabditis elegans, respectively. Furthermore, we report the differential association of mRNA-binding proteins (mRPBs) upon induction of apoptosis in C. elegans L4-stage larvae. Strikingly, most proteins composing mRBPomes, including components of early metabolic pathways and the proteasome, are evolutionarily conserved between yeast and C. elegans. We speculate, on the basis of our evidence that glycolytic enzymes bind distinct glycolytic mRNAs, that enzyme-mRNA interactions relate to an ancient mechanism for post-transcriptional coordination of metabolic pathways that perhaps was established during the transition from the early 'RNA world' to the 'protein world'.
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