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Molecular basis for the specific and multivariant recognitions of RNA substrates by human hnRNP A2/B1.

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Wu B, Su S, Patil DP, Liu H, Gan J, Jaffrey SR, Ma J
OpenAccess logo Nat Commun 9 420 (2018)
Related entries: 5ho4, 5wwe, 5wwg

Cited: 180 times
EuropePMC logo PMID: 29379020

Abstract

Human hnRNP A2/B1 is an RNA-binding protein that plays important roles in many biological processes, including maturation, transport, and metabolism of mRNA, and gene regulation of long noncoding RNAs. hnRNP A2/B1 was reported to control the microRNAs sorting to exosomes and promote primary microRNA processing as a potential m6A "reader." hnRNP A2/B1 contains two RNA recognition motifs that provide sequence-specific recognition of RNA substrates. Here, we determine crystal structures of tandem RRM domains of hnRNP A2/B1 in complex with various RNA substrates, elucidating specific recognitions of AGG and UAG motifs by RRM1 and RRM2 domains, respectively. Further structural and biochemical results demonstrate multivariant binding modes for sequence-diversified RNA substrates, supporting a RNA matchmaker mechanism in hnRNP A2/B1 function. Moreover, our studies in combination with bioinformatic analysis suggest that hnRNP A2/B1 may mediate effects of m6A through a "m6A switch" mechanism, instead of acting as a direct "reader" of m6A modification.

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