Proteomics,Multiomics

Dataset Information

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Zc3h13/Flacc is required for adenosine methylation by bridging the mRNA binding factor Rbm15/Spenito to other components of the m6A machinery


ABSTRACT: N6-methyladenosine (m6A) is an abundant RNA 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, Flacc controls m6A levels and is involved in sex determination in Drosophila. We demonstrate that Flacc promotes the recruitment of the methyltransferase to mRNA by bridging Fl(2)d to the mRNA binding factor Spenito. Altogether, our work advances our molecular understanding of conservation and regulation of the m6A machinery.

OTHER RELATED OMICS DATASETS IN: GSE106614GSE105900

INSTRUMENT(S): Orbitrap Fusion, Q Exactive Plus

ORGANISM(S): Drosophila Melanogaster (fruit Fly) Mus Musculus (mouse)

TISSUE(S): Cell Culture, Embryonic Stem Cell

SUBMITTER: Daniel Hess  

LAB HEAD: Marc Bühler

PROVIDER: PXD008111 | Pride | 2018-12-20

REPOSITORIES: Pride

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Publications

Zc3h13/Flacc is required for adenosine methylation by bridging the mRNA-binding factor Rbm15/Spenito to the m<sup>6</sup>A machinery component Wtap/Fl(2)d.

Knuckles Philip P   Lence Tina T   Haussmann Irmgard U IU   Jacob Dominik D   Kreim Nastasja N   Carl Sarah H SH   Masiello Irene I   Hares Tina T   Villaseñor Rodrigo R   Hess Daniel D   Andrade-Navarro Miguel A MA   Biggiogera Marco M   Helm Mark M   Soller Matthias M   Bühler Marc M   Roignant Jean-Yves JY  

Genes & development 20180313 5-6


<i>N</i><sup>6</sup>-methyladenosine (m<sup>6</sup>A) is the most abundant mRNA modification in eukaryotes, playing crucial roles in multiple biological processes. m<sup>6</sup>A is catalyzed by the activity of methyltransferase-like 3 (Mettl3), which depends on additional proteins whose precise functions remain poorly understood. Here we identified Zc3h13 (zinc finger CCCH domain-containing protein 13)/Flacc [Fl(2)d-associated complex component] as a novel interactor of m<sup>6</sup>A methyltra  ...[more]

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