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Molecular basis for the specific and multivariant recognitions of RNA substrates by human hnRNP A2/B1
Open accessAbstract
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 m 6 A “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 m 6 A through a “m 6 A switch” mechanism, instead of acting as a direct “reader” of m 6 A modification.
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Metadata
- Authors
- Wu, B., Su, S., Patil, D. P., Liu, H., Gan, J., Jaffrey, S. R., & Ma, J.
- Venue
- Nature Communications
- Published
- 2018-01-29
- Volume
- 9
- Issue
- 1
- Pages
- 420-420
- ISSN
- 2041-1723 (ISSN-L)
- OpenAlex
- W2620642044
- Cited by
- 391
- References
- 50
- FWCI
- 10.75
- Type
- journal article
- Language
- en
- Open access
- gold
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- Wu, B., Su, S., Patil, D. P., Liu, H., Gan, J., Jaffrey, S. R., & Ma, J. (2018). Molecular basis for the specific and multivariant recognitions of RNA substrates by human hnRNP A2/B1. Nature Communications. https://doi.org/10.1038/s41467-017-02770-z
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