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

Yoshiko Maida, Mami Yasukawa, Miho Furuuchi, Timo Lassmann, Richard Possemato, Naoko Okamoto, Vivi Kasim, Yoshihide Hayashizaki, William C. Hahn () and Kenkichi Masutomi ()
Additional contact information
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
Kenkichi Masutomi: Cancer Stem Cell Project, National Cancer Center Research Institute, 5-1-1 Tsukiji, Chuo-ku, Tokyo 104-0045, Japan

Nature, 2009, vol. 461, issue 7261, 230-235

Abstract: 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.

Date: 2009
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DOI: 10.1038/nature08283

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