ArticleMolecular and cellular biology2004
The Yaf9 component of the SWR1 and NuA4 complexes is required for proper gene expression, histone H4 acetylation, and Htz1 replacement near telomeres.
Article in Molecular and cellular biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.
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Who cites it
70 citing papers in PubMed, 116 citations in OpenAlex.
- Article
- The C-terminal protein interaction domain of the chromatin reader Yaf9 is critical for pathogenesis ofmSphere · 2024Article
- GAS41 promotes H2A.Z deposition through recognition of the N terminus of histone H3 by the YEATS domain.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- SWR1 chromatin remodeling complex prevents mitotic slippage during spindle position checkpoint arrest.Molecular biology of the cell · 2023Article
- Mechanistic insights into genomic structure and functions of a novel oncogene YEATS4.Frontiers in cell and developmental biology · 2023Review
- A balancing act: interactions within NuA4/TIP60 regulate picNuA4 function in Saccharomyces cerevisiae and humans.Genetics · 2022Article
- Recognition of acetylated histone by Yaf9 regulates metabolic cycling of transcription initiation and chromatin regulatory factors.Genes & development · 2021Article
- Genome Organization and Dynamics Specialty Grand Challenge.Frontiers in molecular biosciences · 2021Article
- Swc4 positively regulates telomere length independently of its roles in NuA4 and SWR1 complexes.Nucleic acids research · 2020Article
- Taf14 is required for the stabilization of transcription pre-initiation complex in Saccharomyces cerevisiae.Epigenetics & chromatin · 2020Article
- Roles of the INO80 and SWR1 Chromatin Remodeling Complexes in Plants.International journal of molecular sciences · 2019Review
- Arabidopsis SWR1-associated protein methyl-CpG-binding domain 9 is required for histone H2A.Z deposition.Nature communications · 2019Article
- Yaf9 subunit of the NuA4 and SWR1 complexes targets histone H3K27ac through its YEATS domain.Nucleic acids research · 2018Article
- Merge and separation of NuA4 and SWR1 complexes control cell fate plasticity inCell discovery · 2018Article
- Phosphorylation of Histone H2A at Serine 95: A Plant-Specific Mark Involved in Flowering Time Regulation and H2A.Z Deposition.The Plant cell · 2017Article
- Composition and Function of Mutant Swi/Snf Complexes.Cell reports · 2017Article
- Loss of Snf5 Induces Formation of an Aberrant SWI/SNF Complex.Cell reports · 2017Article
- Histone H3K36 methylation regulates pre-mRNA splicing in Saccharomyces cerevisiae.RNA biology · 2016Article
- Association of Taf14 with acetylated histone H3 directs gene transcription and the DNA damage response.Genes & development · 2015Article
- Eaf1p Is Required for Recruitment of NuA4 in Targeting TFIID to the Promoters of the Ribosomal Protein Genes for Transcriptional Initiation In Vivo.Molecular and cellular biology · 2015Article
10 more citing papers are in PubMed but not listed here.
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
Yaf9, Taf14, and Sas5 comprise the YEATS domain family in Saccharomyces cerevisiae, which in humans includes proteins involved in acute leukemias. The YEATS domain family is essential, as a yaf9Delta taf14Delta sas5Delta triple mutant is nonviable. We verify that Yaf9 is a stable component of NuA4, an essential histone H4 acetyltransferase complex. Yaf9 is also associated with the SWR1 complex, which deposits the histone H2A variant Htz1. However, the functional contribution of Yaf9 to these complexes has not been determined. Strains lacking YAF9 are sensitive to DNA-damaging agents, cold, and caffeine, and the YEATS domain is required for full Yaf9 function. NuA4 lacking Yaf9 retains histone acetyltransferase activity in vitro, and Yaf9 does not markedly reduce bulk H4 acetylation levels, suggesting a role for Yaf9 in the targeting or regulation of NuA4. Interestingly, yaf9Delta strains display reduced transcription of genes near certain telomeres, and their repression is correlated with reduced H4 acetylation, reduced occupancy by Htz1, and increased occupancy by the silencing protein Sir3. Additionally, the spectra of phenotypes, genes, and telomeres affected in yaf9Delta and htz1Delta strains are significantly similar, further supporting a role for Yaf9 in Htz1 deposition. Taken together, these data indicate that Yaf9 may function in NuA4 and SWR1 complexes to help antagonize silencing near telomeres.
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