ArticleNucleic acids research2008
Involvement of fission yeast Clr6-HDAC in regulation of the checkpoint kinase Cds1.
Article in Nucleic acids research, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 18 citations in OpenAlex.
- Dissecting the cell cycle regulation, DNA damage sensitivity and lifespan effects of caffeine in fission yeast.Microbial cell (Graz, Austria) · 2025Article
- Mutation in histone deacetylase clr6 promotes the survival of S. pombe cds1 null mutant in response to hydroxyurea.Molecular genetics and genomics : MGG · 2020Article
- The NuA4 acetyltransferase and histone H4 acetylation promote replication recovery after topoisomerase I-poisoning.Epigenetics & chromatin · 2019Article
- Histone H4 acetylation required for chromatin decompaction during DNA replication.Scientific reports · 2015Article
- Pcf1, a large subunit of CAF-1, required for maintenance of checkpoint kinase Cds1 activity.SpringerPlus · 2014Article
- Deacetylase Rpd3 facilitates checkpoint adaptation by preventing Rad53 overactivation.Molecular and cellular biology · 2013Article
- Genome-wide screening for genes associated with valproic acid sensitivity in fission yeast.PloS one · 2013Article
- Autoregulation of convergent RNAi genes in fission yeast.Genes & development · 2011Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Modification of the N-terminal tail of histones is required for various nuclear processes. Here, we show that fission yeast Clr6-HDAC (histone deacetylase) regulates the checkpoint kinase Cds1 when DNA replication encounters a stressful condition. We found that the global level of acetylation of histone H4 was constant throughout the normal cell cycle, but was reduced significantly when the cell recovered from the HU-induced cell cycle arrest (or slow DNA replication). We identified the Clr6-HDAC as a component responsible for the reduction in the level of the H4 acetylation. Although DNA replication was completed, the HU-induced cell cycle arrest could not be released even after removal of HU in the clr6-1 mutant. Under this experimental condition, Cds1 kinase was maintained active and remained bound tightly to chromatin. We also demonstrated that Cds1 was active even after treatment with caffeine, an inhibitor for ATM/ATR that is an activator of Cds1. These results indicate that inactivation of Cds1 requires functional Clr6-HDAC independently of the conventional DNA replication checkpoint. When DNA replication is impeded, Clr6-HDAC activity may monitor damage on chromatin structure/environment, which is required for inactivation of Cds1.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.