Rif2 protects Rap1-depleted telomeres from MRX-mediated degradation in Saccharomyces cerevisiae
(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
- Rosas Bringas, Fernando Rodrigo ; Stinus, Sonia ; de Zoeten, Pien ; Cohn, Marita LU and Chang, Michael
- organization
- publishing date
- 2022-01
- 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
- 2024-09-19 19:58:01
@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}}, }