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The methyl phosphate capping enzyme Bmc1/Bin3 is a stable component of the fission yeast telomerase holoenzyme

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  • Jennifer Porat

    (York University)

  • Moaine El Baidouri

    (LGDP-UMR5096, Université de Perpignan Via Domitia
    CNRS LGDP-UMR5096)

  • Jorg Grigull

    (York University)

  • Jean-Marc Deragon

    (LGDP-UMR5096, Université de Perpignan Via Domitia
    CNRS LGDP-UMR5096
    Institut Universitaire de France)

  • Mark A. Bayfield

    (York University)

Abstract

The telomerase holoenzyme is critical for maintaining eukaryotic genome integrity. In addition to a reverse transcriptase and an RNA template, telomerase contains additional proteins that protect the telomerase RNA and promote holoenzyme assembly. Here we report that the methyl phosphate capping enzyme (MePCE) Bmc1/Bin3 is a stable component of the S. pombe telomerase holoenzyme. Bmc1 associates with the telomerase holoenzyme and U6 snRNA through an interaction with the recently described LARP7 family member Pof8, and we demonstrate that these two factors are evolutionarily linked in fungi. Our data suggest that the association of Bmc1 with telomerase is independent of its methyltransferase activity, but rather that Bmc1 functions in telomerase holoenzyme assembly by promoting TER1 accumulation and Pof8 recruitment to TER1. Taken together, this work yields new insight into the composition, assembly, and regulation of the telomerase holoenzyme in fission yeast as well as the breadth of its evolutionary conservation.

Suggested Citation

  • Jennifer Porat & Moaine El Baidouri & Jorg Grigull & Jean-Marc Deragon & Mark A. Bayfield, 2022. "The methyl phosphate capping enzyme Bmc1/Bin3 is a stable component of the fission yeast telomerase holoenzyme," Nature Communications, Nature, vol. 13(1), pages 1-14, December.
    • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-28985-3
    DOI: 10.1038/s41467-022-28985-3
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    References listed on IDEAS

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    1. Chi-Kang Tseng & Hui-Fang Wang & Morgan R. Schroeder & Peter Baumann, 2018. "The H/ACA complex disrupts triplex in hTR precursor to permit processing by RRP6 and PARN," Nature Communications, Nature, vol. 9(1), pages 1-12, December.
    2. Zhiyuan Yang & Qingwei Zhu & Kunxin Luo & Qiang Zhou, 2001. "The 7SK small nuclear RNA inhibits the CDK9/cyclin T1 kinase to control transcription," Nature, Nature, vol. 414(6861), pages 317-322, November.
    3. Amanda K. Mennie & Bettina A. Moser & Toru M. Nakamura, 2018. "LARP7-like protein Pof8 regulates telomerase assembly and poly(A)+TERRA expression in fission yeast," Nature Communications, Nature, vol. 9(1), pages 1-12, December.
    4. Laura C. Collopy & Tracy L. Ware & Tomas Goncalves & Sunnvør í Kongsstovu & Qian Yang & Hanna Amelina & Corinne Pinder & Ala Alenazi & Vera Moiseeva & Siân R. Pearson & Christine A. Armstrong & Kazuno, 2018. "LARP7 family proteins have conserved function in telomerase assembly," Nature Communications, Nature, vol. 9(1), pages 1-8, December.
    5. P. Daniela Garcia & Robert W. Leach & Gable M. Wadsworth & Krishna Choudhary & Hua Li & Sharon Aviran & Harold D. Kim & Virginia A. Zakian, 2020. "Stability and nuclear localization of yeast telomerase depend on protein components of RNase P/MRP," Nature Communications, Nature, vol. 11(1), pages 1-19, December.
    6. Van Trung Nguyen & Tamás Kiss & Annemieke A. Michels & Olivier Bensaude, 2001. "7SK small nuclear RNA binds to and inhibits the activity of CDK9/cyclin T complexes," Nature, Nature, vol. 414(6861), pages 322-325, November.
    7. Wen Tang & Ram Kannan & Marco Blanchette & Peter Baumann, 2012. "Telomerase RNA biogenesis involves sequential binding by Sm and Lsm complexes," Nature, Nature, vol. 484(7393), pages 260-264, April.
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    1. Tsai-Ling Kao & Yu-Cheng Huang & Yi-Hsuan Chen & Peter Baumann & Chi-Kang Tseng, 2024. "LARP3, LARP7, and MePCE are involved in the early stage of human telomerase RNA biogenesis," Nature Communications, Nature, vol. 15(1), pages 1-16, December.

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