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LARP7 family proteins have conserved function in telomerase assembly
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...
Autores principales: | , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group UK
2018
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5805788/ https://www.ncbi.nlm.nih.gov/pubmed/29422501 http://dx.doi.org/10.1038/s41467-017-02296-4 |
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author | Collopy, Laura C. Ware, Tracy L. Goncalves, Tomas í Kongsstovu, Sunnvør Yang, Qian Amelina, Hanna Pinder, Corinne Alenazi, Ala Moiseeva, Vera Pearson, Siân R. Armstrong, Christine A. Tomita, Kazunori |
author_facet | Collopy, Laura C. Ware, Tracy L. Goncalves, Tomas í Kongsstovu, Sunnvør Yang, Qian Amelina, Hanna Pinder, Corinne Alenazi, Ala Moiseeva, Vera Pearson, Siân R. Armstrong, Christine A. Tomita, Kazunori |
author_sort | Collopy, Laura C. |
collection | PubMed |
description | 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. |
format | Online Article Text |
id | pubmed-5805788 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2018 |
publisher | Nature Publishing Group UK |
record_format | MEDLINE/PubMed |
spelling | pubmed-58057882018-02-12 LARP7 family proteins have conserved function in telomerase assembly Collopy, Laura C. Ware, Tracy L. Goncalves, Tomas í Kongsstovu, Sunnvør Yang, Qian Amelina, Hanna Pinder, Corinne Alenazi, Ala Moiseeva, Vera Pearson, Siân R. Armstrong, Christine A. Tomita, Kazunori Nat Commun Article 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. Nature Publishing Group UK 2018-02-08 /pmc/articles/PMC5805788/ /pubmed/29422501 http://dx.doi.org/10.1038/s41467-017-02296-4 Text en © The Author(s) 2018 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. |
spellingShingle | Article Collopy, Laura C. Ware, Tracy L. Goncalves, Tomas í Kongsstovu, Sunnvør Yang, Qian Amelina, Hanna Pinder, Corinne Alenazi, Ala Moiseeva, Vera Pearson, Siân R. Armstrong, Christine A. Tomita, Kazunori LARP7 family proteins have conserved function in telomerase assembly |
title | LARP7 family proteins have conserved function in telomerase assembly |
title_full | LARP7 family proteins have conserved function in telomerase assembly |
title_fullStr | LARP7 family proteins have conserved function in telomerase assembly |
title_full_unstemmed | LARP7 family proteins have conserved function in telomerase assembly |
title_short | LARP7 family proteins have conserved function in telomerase assembly |
title_sort | larp7 family proteins have conserved function in telomerase assembly |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5805788/ https://www.ncbi.nlm.nih.gov/pubmed/29422501 http://dx.doi.org/10.1038/s41467-017-02296-4 |
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