Background: Human YT521-B homology (YTH) domain selectively recognizes N6-methyladenosine (m6A) RNA.Results: YTHDF1 and Pho92 recognize m6A without sequence preference.Conclusion: The structure of YTHDF1 explained the key residue difference that results in the weaker binding of YTHDF1-3 compared with YTHDC1.Significance: This study systematically investigated the binding characteristics of the human YTH domain proteins, as well as yeast Pho92, and indicated the discriminative recognition of m6A among different YTH domains.
