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Swc4 protects nucleosome-free rDNA, tDNA and telomere loci to inhibit genome instability.
- Source :
-
DNA repair [DNA Repair (Amst)] 2023 Jul; Vol. 127, pp. 103512. Date of Electronic Publication: 2023 May 18. - Publication Year :
- 2023
-
Abstract
- In the baker's yeast Saccharomyces cerevisiae, NuA4 and SWR1-C, two multisubunit complexes, are involved in histone acetylation and chromatin remodeling, respectively. Eaf1 is the assembly platform subunit of NuA4, Swr1 is the assembly platform and catalytic subunit of SWR1-C, while Swc4, Yaf9, Arp4 and Act1 form a functional module, and is present in both NuA4 and SWR1 complexes. ACT1 and ARP4 are essential for cell survival. Deletion of SWC4, but not YAF9, EAF1 or SWR1 results in a severe growth defect, but the underlying mechanism remains largely unknown. Here, we show that swc4Δ, but not yaf9Δ, eaf1Δ, or swr1Δ cells display defects in DNA ploidy and chromosome segregation, suggesting that the defects observed in swc4Δ cells are independent of NuA4 or SWR1-C integrity. Swc4 is enriched in the nucleosome-free regions (NFRs) of the genome, including characteristic regions of RDN5s, tDNAs and telomeres, independently of Yaf9, Eaf1 or Swr1. In particular, rDNA, tDNA and telomere loci are more unstable and prone to recombination in the swc4Δ cells than in wild-type cells. Taken together, we conclude that the chromatin associated Swc4 protects nucleosome-free chromatin of rDNA, tDNA and telomere loci to ensure genome integrity.<br />Competing Interests: Declaration of Competing Interest The authors declare that there are no conflicts of interest.<br /> (Copyright © 2023 Elsevier B.V. All rights reserved.)
- Subjects :
- Humans
Histones metabolism
DNA, Ribosomal
Chromatin
Saccharomyces cerevisiae genetics
Saccharomyces cerevisiae metabolism
Telomere genetics
Telomere metabolism
Genomic Instability
Chromatin Assembly and Disassembly
Histone Acetyltransferases genetics
Transcription Factors genetics
Nucleosomes
Saccharomyces cerevisiae Proteins genetics
Saccharomyces cerevisiae Proteins metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1568-7856
- Volume :
- 127
- Database :
- MEDLINE
- Journal :
- DNA repair
- Publication Type :
- Academic Journal
- Accession number :
- 37230009
- Full Text :
- https://doi.org/10.1016/j.dnarep.2023.103512