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TENT2, TUT4, and TUT7 selectively regulate miRNA sequence and abundance

Author

Listed:
  • Acong Yang

    (National Cancer Institute)

  • Xavier Bofill-De Ros

    (National Cancer Institute)

  • Ryan Stanton

    (National Cancer Institute)

  • Tie-Juan Shao

    (National Cancer Institute
    Zhejiang Chinese Medical University)

  • Patricia Villanueva

    (National Cancer Institute)

  • Shuo Gu

    (National Cancer Institute)

Abstract

TENTs generate miRNA isoforms by 3’ tailing. However, little is known about how tailing regulates miRNA function. Here, we generate isogenic HEK293T cell lines in which TENT2, TUT4 and TUT7 are knocked out individually or in combination. Together with rescue experiments, we characterize TENT-specific effects by deep sequencing, Northern blot and in vitro assays. We find that 3’ tailing is not random but highly specific. In addition to its known adenylation, TENT2 contributes to guanylation and uridylation on mature miRNAs. TUT4 uridylates most miRNAs whereas TUT7 is dispensable. Removing adenylation has a marginal impact on miRNA levels. By contrast, abolishing uridylation leads to dysregulation of a set of miRNAs. Besides let-7, miR-181b and miR-222 are negatively regulated by TUT4/7 via distinct mechanisms while the miR-888 cluster is upregulated specifically by TUT7. Our results uncover the selective actions of TENTs in generating 3’ isomiRs and pave the way to investigate their functions.

Suggested Citation

  • Acong Yang & Xavier Bofill-De Ros & Ryan Stanton & Tie-Juan Shao & Patricia Villanueva & Shuo Gu, 2022. "TENT2, TUT4, and TUT7 selectively regulate miRNA sequence and abundance," Nature Communications, Nature, vol. 13(1), pages 1-15, December.
    • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-32969-8
    DOI: 10.1038/s41467-022-32969-8
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    References listed on IDEAS

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    1. Acong Yang & Tie-Juan Shao & Xavier Bofill-De Ros & Chuanjiang Lian & Patricia Villanueva & Lisheng Dai & Shuo Gu, 2020. "AGO-bound mature miRNAs are oligouridylated by TUTs and subsequently degraded by DIS3L2," Nature Communications, Nature, vol. 11(1), pages 1-13, December.
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