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

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Listed:
  • Baixing Wu

    (Fudan University)

  • Shichen Su

    (Fudan University)

  • Deepak P. Patil

    (Cornell University)

  • Hehua Liu

    (Fudan University
    Fudan University)

  • Jianhua Gan

    (Fudan University)

  • Samie R. Jaffrey

    (Cornell University)

  • Jinbiao Ma

    (Fudan University)

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.

Suggested Citation

  • Baixing Wu & Shichen Su & Deepak P. Patil & Hehua Liu & Jianhua Gan & Samie R. Jaffrey & Jinbiao Ma, 2018. "Molecular basis for the specific and multivariant recognitions of RNA substrates by human hnRNP A2/B1," Nature Communications, Nature, vol. 9(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-017-02770-z
    DOI: 10.1038/s41467-017-02770-z
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    Cited by:

    1. Cristina Leoni & Marian Bataclan & Taku Ito-Kureha & Vigo Heissmeyer & Silvia Monticelli, 2023. "The mRNA methyltransferase Mettl3 modulates cytokine mRNA stability and limits functional responses in mast cells," Nature Communications, Nature, vol. 14(1), pages 1-17, December.

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