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

Baixing Wu, Shichen Su, Deepak P. Patil, Hehua Liu, Jianhua Gan, Samie R. Jaffrey and Jinbiao Ma ()
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Baixing Wu: Fudan University
Shichen Su: Fudan University
Deepak P. Patil: Cornell University
Hehua Liu: Fudan University
Jianhua Gan: Fudan University
Samie R. Jaffrey: Cornell University
Jinbiao Ma: Fudan University

Nature Communications, 2018, vol. 9, issue 1, 1-12

Abstract: 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.

Date: 2018
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DOI: 10.1038/s41467-017-02770-z

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