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LARP7 family proteins have conserved function in telomerase assembly

Author

Listed:
  • Laura C. Collopy

    (University College London)

  • Tracy L. Ware

    (University College London
    Salem State University)

  • Tomas Goncalves

    (University College London
    University College London)

  • Sunnvør í Kongsstovu

    (University College London
    Imperial College London)

  • Qian Yang

    (University College London)

  • Hanna Amelina

    (University College London)

  • Corinne Pinder

    (University College London
    University College London)

  • Ala Alenazi

    (University College London
    Imperial College London)

  • Vera Moiseeva

    (University College London)

  • Siân R. Pearson

    (University College London)

  • Christine A. Armstrong

    (University College London)

  • Kazunori Tomita

    (University College London)

Abstract

Understanding the intricacies of telomerase regulation is crucial due to the potential health benefits of modifying its activity. Telomerase is composed of an RNA component and reverse transcriptase. However, additional factors required during biogenesis vary between species. Here we have identified fission yeast Lar7 as a member of the conserved LARP7 family, which includes the Tetrahymena telomerase-binding protein p65 and human LARP7. We show that Lar7 has conserved RNA-recognition motifs, which bind telomerase RNA to protect it from exosomal degradation. In addition, Lar7 is required to stabilise the association of telomerase RNA with the protective complex LSm2–8, and telomerase reverse transcriptase. Lar7 remains a component of the mature telomerase complex and is required for telomerase localisation to the telomere. Collectively, we demonstrate that Lar7 is a crucial player in fission yeast telomerase biogenesis, similarly to p65 in Tetrahymena, and highlight the LARP7 family as a conserved factor in telomere maintenance.

Suggested Citation

  • 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.
    • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-017-02296-4
    DOI: 10.1038/s41467-017-02296-4
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    Cited by:

    1. 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.
    2. 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.
    3. Diego J. Páez-Moscoso & David V. Ho & Lili Pan & Katie Hildebrand & Kristi L. Jensen & Michaella J. Levy & Laurence Florens & Peter Baumann, 2022. "A putative cap binding protein and the methyl phosphate capping enzyme Bin3/MePCE function in telomerase biogenesis," Nature Communications, Nature, vol. 13(1), pages 1-16, December.

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