M6A in 5’ untranslated regions promotes cap-independent translation of mRNA

ABSTRACT: N6-methyladenosine (m6A) is a widespread internal RNA modification whose function is poorly understood. Here we report that m6A residues within the 5'UTR promote a novel form of cap-independent translation which is mediated through an interaction between m6A residues and the translation initiation factor, eIF3. We present eIF3a PAR-iCLIP data which demonstrate that eIF3 predominantly binds mRNAs within the 5'UTR. eIF3 binding sites are also in proximity to m6A residues within the 5'UTR of cellular mRNAs. Two replicates of eIF3a PAR-iCLIP in HEK293T cells.

ORGANISM(S): Homo sapiens

SUBMITTER: Kate Meyer 

PROVIDER: E-GEOD-73405 | biostudies-arrayexpress |

REPOSITORIES: biostudies-arrayexpress