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Rif2 protects Rap1-depleted telomeres from MRX-mediated degradation in Saccharomyces cerevisiae

Rosas Bringas, Fernando Rodrigo ; Stinus, Sonia ; de Zoeten, Pien ; Cohn, Marita LU and Chang, Michael (2022) In eLife 11.
Abstract

Rap1 is the main protein that binds double-stranded telomeric DNA in Saccharomyces cerevisiae. Examination of the telomere functions of Rap1 is complicated by the fact that it also acts as a transcriptional regulator of hundreds of genes and is encoded by an essential gene. In this study, we disrupt Rap1 telomere association by expressing a mutant telomerase RNA subunit (tlc1-tm) that introduces mutant telomeric repeats. tlc1-tm cells grow similar to wild-type cells, although depletion of Rap1 at telomeres causes defects in telomere length regulation and telomere capping. Rif2 is a protein normally recruited to telomeres by Rap1, but we show that Rif2 can still associate with Rap1-depleted tlc1-tm telomeres, and that this association is... (More)

Rap1 is the main protein that binds double-stranded telomeric DNA in Saccharomyces cerevisiae. Examination of the telomere functions of Rap1 is complicated by the fact that it also acts as a transcriptional regulator of hundreds of genes and is encoded by an essential gene. In this study, we disrupt Rap1 telomere association by expressing a mutant telomerase RNA subunit (tlc1-tm) that introduces mutant telomeric repeats. tlc1-tm cells grow similar to wild-type cells, although depletion of Rap1 at telomeres causes defects in telomere length regulation and telomere capping. Rif2 is a protein normally recruited to telomeres by Rap1, but we show that Rif2 can still associate with Rap1-depleted tlc1-tm telomeres, and that this association is required to inhibit telomere degradation by the MRX complex. Rif2 and the Ku complex work in parallel to prevent tlc1-tm telo-mere degradation; tlc1-tm cells lacking Rif2 and the Ku complex are inviable. The partially redundant mechanisms may explain the rapid evolution of telomere components in budding yeast species.

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author
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publishing date
type
Contribution to journal
publication status
published
subject
in
eLife
volume
11
article number
e74090
publisher
eLife Sciences Publications
external identifiers
  • scopus:85123734176
  • pmid:35044907
ISSN
2050-084X
DOI
10.7554/eLife.74090
language
English
LU publication?
yes
additional info
Publisher Copyright: © Rosas Bringas et al.
id
2d03350d-c8f8-4424-a602-520604c2ec82
date added to LUP
2022-02-16 14:03:21
date last changed
2024-06-13 10:45:19
@article{2d03350d-c8f8-4424-a602-520604c2ec82,
  abstract     = {{<p>Rap1 is the main protein that binds double-stranded telomeric DNA in Saccharomyces cerevisiae. Examination of the telomere functions of Rap1 is complicated by the fact that it also acts as a transcriptional regulator of hundreds of genes and is encoded by an essential gene. In this study, we disrupt Rap1 telomere association by expressing a mutant telomerase RNA subunit (tlc1-tm) that introduces mutant telomeric repeats. tlc1-tm cells grow similar to wild-type cells, although depletion of Rap1 at telomeres causes defects in telomere length regulation and telomere capping. Rif2 is a protein normally recruited to telomeres by Rap1, but we show that Rif2 can still associate with Rap1-depleted tlc1-tm telomeres, and that this association is required to inhibit telomere degradation by the MRX complex. Rif2 and the Ku complex work in parallel to prevent tlc1-tm telo-mere degradation; tlc1-tm cells lacking Rif2 and the Ku complex are inviable. The partially redundant mechanisms may explain the rapid evolution of telomere components in budding yeast species.</p>}},
  author       = {{Rosas Bringas, Fernando Rodrigo and Stinus, Sonia and de Zoeten, Pien and Cohn, Marita and Chang, Michael}},
  issn         = {{2050-084X}},
  language     = {{eng}},
  publisher    = {{eLife Sciences Publications}},
  series       = {{eLife}},
  title        = {{Rif2 protects Rap1-depleted telomeres from MRX-mediated degradation in Saccharomyces cerevisiae}},
  url          = {{http://dx.doi.org/10.7554/eLife.74090}},
  doi          = {{10.7554/eLife.74090}},
  volume       = {{11}},
  year         = {{2022}},
}