Zc3h13/Flacc is required for adenosine methylation by bridging the mRNA binding factor Rbm15/Spenito to the m6A machinery component Wtap/Fl(2)d

Research output: Contribution to journalArticlepeer-review


  • P Knuckles
  • T Lence
  • D Jacob
  • N Kreim
  • SH Carl
  • I Masiello
  • T Hares
  • R Villasenior
  • D Hess
  • MA Andrade-Navarro
  • M Biggiogera
  • M Helm
  • M Buhler
  • JY Roignant

Colleges, School and Institutes

External organisations

  • Friedrich Miescher Institute for Biomedical Research, Maulbeerstrasse 66, 4058 Basel, Switzerland
  • Laboratory of RNA Epigenetics, Institute of Molecular Biology (IMB), Mainz, 55128, Germany
  • Institute of Pharmacy and Biochemistry, Johannes Gutenberg University of Mainz, 55128 Mainz, Germany
  • Genomic core facility, Institute of Molecular Biology (IMB), Mainz, 55128, Germany
  • Laboratory of Cell Biology and Neurobiology, Department of Animal Biology, University of Pavia, Pavia, Italy.


N6-methyladenosine (m6A) is the most abundant mRNA modification in eukaryotes, playing crucial roles in multiple biological processes. m6A is catalyzed by the activity of Mettl3, which depends on additional proteins whose precise functions remain poorly understood. Here we identified Flacc/Zc3h13 as a novel interactor of m6A methyltransferase complex components in Drosophila and mouse. Like other components of this complex, Flacc controls m6A levels and is involved in sex determination in Drosophila. We demonstrate that Flacc promotes m6A deposition by bridging Fl(2)d to the mRNA binding factor Nito. Altogether, our work advances our molecular understanding of conservation and regulation of the m6A machinery.


Original languageEnglish
JournalGenes & Development
Early online date13 Mar 2018
Publication statusE-pub ahead of print - 13 Mar 2018