LARP7 family proteins have conserved function in telomerase assembly

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 and Kazunori Tomita ()
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Laura C. Collopy: University College London
Tracy L. Ware: University College London
Tomas Goncalves: University College London
Sunnvør í Kongsstovu: University College London
Qian Yang: University College London
Hanna Amelina: University College London
Corinne Pinder: University College London
Ala Alenazi: University College London
Vera Moiseeva: University College London
Siân R. Pearson: University College London
Christine A. Armstrong: University College London
Kazunori Tomita: University College London

Nature Communications, 2018, vol. 9, issue 1, 1-8

Abstract: 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.

Date: 2018
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DOI: 10.1038/s41467-017-02296-4

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