On the specificity of the recognition of m6A-RNA by YTH reader domains.

ABSTRACT: Most processes of life are the result of polyvalent interactions between macromolecules, often of heterogeneous types and sizes. Frequently, the times associated with these interactions are prohibitively long for interrogation using atomistic simulations. Here, we study the recognition of N6-methylated adenine (m⁶A) in RNA by the reader domain YTHDC1, a prototypical, cognate pair that challenges simulations through its composition and required timescales. Simulations of RNA pentanucleotides in water reveal that the unbound state can impact (un)binding kinetics in a manner that is both model- and sequence-dependent. This is important because there are two contributions to the specificity of the recognition of the Gm⁶AC motif: from the sequence adjacent to the central a

SUBMITTER: Widmer J 

PROVIDER: S-EPMC11699332 | biostudies-literature | 2024 Dec

REPOSITORIES: biostudies-literature