Cargando…

The RNA-binding proteomes from yeast to man harbour conserved enigmRBPs

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...

Descripción completa

Detalles Bibliográficos
Autores principales: Beckmann, Benedikt M., Horos, Rastislav, Fischer, Bernd, Castello, Alfredo, Eichelbaum, Katrin, Alleaume, Anne-Marie, Schwarzl, Thomas, Curk, Tomaž, Foehr, Sophia, Huber, Wolfgang, Krijgsveld, Jeroen, Hentze, Matthias W.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4686815/
https://www.ncbi.nlm.nih.gov/pubmed/26632259
http://dx.doi.org/10.1038/ncomms10127
_version_ 1782406504504098816
author Beckmann, Benedikt M.
Horos, Rastislav
Fischer, Bernd
Castello, Alfredo
Eichelbaum, Katrin
Alleaume, Anne-Marie
Schwarzl, Thomas
Curk, Tomaž
Foehr, Sophia
Huber, Wolfgang
Krijgsveld, Jeroen
Hentze, Matthias W.
author_facet Beckmann, Benedikt M.
Horos, Rastislav
Fischer, Bernd
Castello, Alfredo
Eichelbaum, Katrin
Alleaume, Anne-Marie
Schwarzl, Thomas
Curk, Tomaž
Foehr, Sophia
Huber, Wolfgang
Krijgsveld, Jeroen
Hentze, Matthias W.
author_sort Beckmann, Benedikt M.
collection PubMed
description 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.
format Online
Article
Text
id pubmed-4686815
institution National Center for Biotechnology Information
language English
publishDate 2015
publisher Nature Publishing Group
record_format MEDLINE/PubMed
spelling pubmed-46868152016-01-07 The RNA-binding proteomes from yeast to man harbour conserved enigmRBPs Beckmann, Benedikt M. Horos, Rastislav Fischer, Bernd Castello, Alfredo Eichelbaum, Katrin Alleaume, Anne-Marie Schwarzl, Thomas Curk, Tomaž Foehr, Sophia Huber, Wolfgang Krijgsveld, Jeroen Hentze, Matthias W. Nat Commun Article 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. Nature Publishing Group 2015-12-03 /pmc/articles/PMC4686815/ /pubmed/26632259 http://dx.doi.org/10.1038/ncomms10127 Text en Copyright © 2015, Nature Publishing Group, a division of Macmillan Publishers Limited. All Rights Reserved. http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article's Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/
spellingShingle Article
Beckmann, Benedikt M.
Horos, Rastislav
Fischer, Bernd
Castello, Alfredo
Eichelbaum, Katrin
Alleaume, Anne-Marie
Schwarzl, Thomas
Curk, Tomaž
Foehr, Sophia
Huber, Wolfgang
Krijgsveld, Jeroen
Hentze, Matthias W.
The RNA-binding proteomes from yeast to man harbour conserved enigmRBPs
title The RNA-binding proteomes from yeast to man harbour conserved enigmRBPs
title_full The RNA-binding proteomes from yeast to man harbour conserved enigmRBPs
title_fullStr The RNA-binding proteomes from yeast to man harbour conserved enigmRBPs
title_full_unstemmed The RNA-binding proteomes from yeast to man harbour conserved enigmRBPs
title_short The RNA-binding proteomes from yeast to man harbour conserved enigmRBPs
title_sort rna-binding proteomes from yeast to man harbour conserved enigmrbps
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4686815/
https://www.ncbi.nlm.nih.gov/pubmed/26632259
http://dx.doi.org/10.1038/ncomms10127
work_keys_str_mv AT beckmannbenediktm thernabindingproteomesfromyeasttomanharbourconservedenigmrbps
AT horosrastislav thernabindingproteomesfromyeasttomanharbourconservedenigmrbps
AT fischerbernd thernabindingproteomesfromyeasttomanharbourconservedenigmrbps
AT castelloalfredo thernabindingproteomesfromyeasttomanharbourconservedenigmrbps
AT eichelbaumkatrin thernabindingproteomesfromyeasttomanharbourconservedenigmrbps
AT alleaumeannemarie thernabindingproteomesfromyeasttomanharbourconservedenigmrbps
AT schwarzlthomas thernabindingproteomesfromyeasttomanharbourconservedenigmrbps
AT curktomaz thernabindingproteomesfromyeasttomanharbourconservedenigmrbps
AT foehrsophia thernabindingproteomesfromyeasttomanharbourconservedenigmrbps
AT huberwolfgang thernabindingproteomesfromyeasttomanharbourconservedenigmrbps
AT krijgsveldjeroen thernabindingproteomesfromyeasttomanharbourconservedenigmrbps
AT hentzematthiasw thernabindingproteomesfromyeasttomanharbourconservedenigmrbps
AT beckmannbenediktm rnabindingproteomesfromyeasttomanharbourconservedenigmrbps
AT horosrastislav rnabindingproteomesfromyeasttomanharbourconservedenigmrbps
AT fischerbernd rnabindingproteomesfromyeasttomanharbourconservedenigmrbps
AT castelloalfredo rnabindingproteomesfromyeasttomanharbourconservedenigmrbps
AT eichelbaumkatrin rnabindingproteomesfromyeasttomanharbourconservedenigmrbps
AT alleaumeannemarie rnabindingproteomesfromyeasttomanharbourconservedenigmrbps
AT schwarzlthomas rnabindingproteomesfromyeasttomanharbourconservedenigmrbps
AT curktomaz rnabindingproteomesfromyeasttomanharbourconservedenigmrbps
AT foehrsophia rnabindingproteomesfromyeasttomanharbourconservedenigmrbps
AT huberwolfgang rnabindingproteomesfromyeasttomanharbourconservedenigmrbps
AT krijgsveldjeroen rnabindingproteomesfromyeasttomanharbourconservedenigmrbps
AT hentzematthiasw rnabindingproteomesfromyeasttomanharbourconservedenigmrbps