The YTH domain is a novel RNA binding domain

Zhaiyi Zhang, Dominik Theler, Katarzyna H. Kaminska, Michael Hiller, Pierre De La Grange, Rainer Pudimat, Ilona Rafalska, Bettina Heinrich, Janusz M. Bujnick, Frédéric H.T. Allain, Stefan Stamm

Research output: Contribution to journalArticlepeer-review

175 Scopus citations

Abstract

The YTH (YT521-B homology) domain was identified by sequence comparison and is found in 174 different proteins expressed in eukaryotes. It is characterized by 14 invariant residues within an α-helix/β-sheet structure. Here we show that the YTH domain is a novel RNA binding domain that binds to a short, degenerated, single-stranded RNA sequence motif. The presence of the binding motif in alternative exons is necessary for YT521-B to directly influence splice site selection in vivo. Array analyses demonstrate that YT521-B predominantly regulates vertebrate-specific exons. An NMR titration experiment identified the binding surface for single-stranded RNA on the YTH domain. Structural analyses indicate that the YTH domain is related to the pseudouridine synthase and archaeosine transglycosylase (PUA) domain. Our data show that the YTH domain conveys RNA binding ability to a new class of proteins that are found in all eukaryotic organisms.

Original languageEnglish
Pages (from-to)14701-14710
Number of pages10
JournalJournal of Biological Chemistry
Volume285
Issue number19
DOIs
StatePublished - May 7 2010

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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