Journal article
The RNA-binding proteomes from yeast to man harbour conserved enigmRBPs
- Abstract:
- RNA-binding proteins (RBPs) exert a broad range of biological functions. To explore the scope of RBPs across eukaryotic evolution, we determined the in vivo RBP repertoire of the yeast Saccharomyces cerevisiae and identified 678 RBPs from yeast and additionally 729 RBPs from human hepatocytic HuH-7 cells. Combined analyses of these and recently published data sets define the core RBP repertoire conserved from yeast to man. Conserved RBPs harbour defined repetitive motifs within disordered regions, which display striking evolutionary expansion. Only 60% of yeast and 73% of the human RBPs have functions assigned to RNA biology or structural motifs known to convey RNA binding, and many intensively studied proteins surprisingly emerge as RBPs (termed ‘enigmRBPs’), including almost all glycolytic enzymes, pointing to emerging connections between gene regulation and metabolism. Analyses of the mitochondrial hydroxysteroid dehydrogenase (HSD17B10) uncover the RNA-binding specificity of an enigmRBP.
- Publication status:
- Published
- Peer review status:
- Peer reviewed
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(Preview, Version of record, pdf, 1.3MB, Terms of use)
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- Publisher copy:
- 10.1038/ncomms10127
Authors
+ German Ministry for Education and Research
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- Funding agency for:
- Hentze, M
- Grant:
- Advanced Grant
+ European Research Council
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- Funding agency for:
- Hentze, M
- Grant:
- Advanced Grant
+ Marie Curie Fellowship
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- Funding agency for:
- Beckmann, B
- Grant:
- FP7/2007-2013/MC-IEF-301031
- Publisher:
- Nature Publishing Group
- Journal:
- Nature Communications More from this journal
- Volume:
- 6
- Publication date:
- 2015-12-03
- Acceptance date:
- 2015-11-05
- DOI:
- EISSN:
-
2041-1723
- Pubs id:
-
pubs:625720
- UUID:
-
uuid:fb2c62a8-f3b7-4570-8797-f6034a67d29d
- Local pid:
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pubs:625720
- Source identifiers:
-
625720
- Deposit date:
-
2016-06-06
Terms of use
- Copyright holder:
- Beckmann et al
- Copyright date:
- 2015
- Notes:
- © 2015 Author(s). This work is licensed under a Creative Commons Attribution 4.0 International License. This is the publisher's version of the article. The final version is available online from Nature Publishing Group at: [10.1038/ncomms10127].
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