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An RNA-dependent RNA polymerase formed by TERT and the RMRP RNA

Author

Listed:
  • Yoshiko Maida

    (Cancer Stem Cell Project, National Cancer Center Research Institute, 5-1-1 Tsukiji, Chuo-ku, Tokyo 104-0045, Japan)

  • Mami Yasukawa

    (Cancer Stem Cell Project, National Cancer Center Research Institute, 5-1-1 Tsukiji, Chuo-ku, Tokyo 104-0045, Japan)

  • Miho Furuuchi

    (Cancer Stem Cell Project, National Cancer Center Research Institute, 5-1-1 Tsukiji, Chuo-ku, Tokyo 104-0045, Japan)

  • Timo Lassmann

    (RIKEN Omics Science Center, RIKEN Yokohama Institute, 1-7-22 Suehiro-cho, Tsurumi-ku, Yokohama 230-0045, Japan)

  • Richard Possemato

    (Brigham and Women’s Hospital and Harvard Medical School, 44 Binney Street, Boston, Massachusetts 02115, USA)

  • Naoko Okamoto

    (Cancer Stem Cell Project, National Cancer Center Research Institute, 5-1-1 Tsukiji, Chuo-ku, Tokyo 104-0045, Japan)

  • Vivi Kasim

    (Cancer Stem Cell Project, National Cancer Center Research Institute, 5-1-1 Tsukiji, Chuo-ku, Tokyo 104-0045, Japan)

  • Yoshihide Hayashizaki

    (RIKEN Omics Science Center, RIKEN Yokohama Institute, 1-7-22 Suehiro-cho, Tsurumi-ku, Yokohama 230-0045, Japan)

  • William C. Hahn

    (Brigham and Women’s Hospital and Harvard Medical School, 44 Binney Street, Boston, Massachusetts 02115, USA
    Broad Institute of Harvard and MIT, 7 Cambridge Center, Cambridge, Massachusetts 02142, USA)

  • Kenkichi Masutomi

    (Cancer Stem Cell Project, National Cancer Center Research Institute, 5-1-1 Tsukiji, Chuo-ku, Tokyo 104-0045, Japan
    PREST, Japan Science and Technology Agency, 4-1-8 Honcho Kawaguchi, Saitama 332-0012, Japan)

Abstract

Constitutive expression of telomerase in human cells prevents the onset of senescence and crisis by maintaining telomere homeostasis. However, accumulating evidence suggests that the human telomerase reverse transcriptase catalytic subunit (TERT) contributes to cell physiology independently of its ability to elongate telomeres. Here we show that TERT interacts with the RNA component of mitochondrial RNA processing endoribonuclease (RMRP), a gene that is mutated in the inherited pleiotropic syndrome cartilage–hair hypoplasia. Human TERT and RMRP form a distinct ribonucleoprotein complex that has RNA-dependent RNA polymerase (RdRP) activity and produces double-stranded RNAs that can be processed into small interfering RNA in a Dicer (also known as DICER1)-dependent manner. These observations identify a mammalian RdRP composed of TERT in complex with RMRP.

Suggested Citation

  • Yoshiko Maida & Mami Yasukawa & Miho Furuuchi & Timo Lassmann & Richard Possemato & Naoko Okamoto & Vivi Kasim & Yoshihide Hayashizaki & William C. Hahn & Kenkichi Masutomi, 2009. "An RNA-dependent RNA polymerase formed by TERT and the RMRP RNA," Nature, Nature, vol. 461(7261), pages 230-235, September.
    • Handle: RePEc:nat:nature:v:461:y:2009:i:7261:d:10.1038_nature08283
    DOI: 10.1038/nature08283
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    Cited by:

    1. Sumirtha Balaratnam & Curran Rhodes & Desta Doro Bume & Colleen Connelly & Christopher C. Lai & James A. Kelley & Kamyar Yazdani & Philip J. Homan & Danny Incarnato & Tomoyuki Numata & John S. Schneek, 2021. "A chemical probe based on the PreQ1 metabolite enables transcriptome-wide mapping of binding sites," Nature Communications, Nature, vol. 12(1), pages 1-15, December.

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