The Yaf9 component of the SWR1 and NuA4 complexes is required for proper gene expression, histone H4 acetylation, and Htz1 replacement near telomeres Journal Article


Authors: Zhang, H.; Richardson, D. O.; Roberts, D. N.; Utley, R.; Erdjument-Bromage, H.; Tempst, P.; Côté, J.; Cairns, B. R.
Article Title: The Yaf9 component of the SWR1 and NuA4 complexes is required for proper gene expression, histone H4 acetylation, and Htz1 replacement near telomeres
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 yaf9Δ taf14Δ sas5Δ triple mutant is nonviable. We verify thai 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, yaf9Δ 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 yaf9Δ and htz1Δ 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.
Keywords: controlled study; unclassified drug; nonhuman; protein function; phenotype; telomere; dna damage; cell division; dna repair; gene expression; protein; protein binding; enzyme activity; correlation analysis; transcription regulation; amino acid sequence; molecular sequence data; saccharomyces cerevisiae; eukaryota; gene repression; temperature; protein structure, tertiary; multiprotein complexes; gene silencing; saccharomyces cerevisiae proteins; multienzyme complex; histone h2a; histones; adenosine triphosphatases; acyltransferase; acetyltransferases; gene expression regulation, fungal; acetylation; dna, fungal; histone h4; fungal strain; caffeine; genes, essential; saccharomyces; histone acetyltransferase; priority journal; article; protein yaf9; silent information regulator protein 2; cold exposure; silent information regulator proteins, saccharomyces cerevisiae
Journal Title: Molecular and Cellular Biology
Volume: 24
Issue: 21
ISSN: 0270-7306
Publisher: American Society for Microbiology  
Date Published: 2004-11-01
Start Page: 9424
End Page: 9436
Language: English
DOI: 10.1128/mcb.24.21.9424-9436.2004
PROVIDER: scopus
PMCID: PMC522225
PUBMED: 15485911
DOI/URL:
Notes: Mol. Cell. Biol. -- Cited By (since 1996):65 -- Export Date: 16 June 2014 -- CODEN: MCEBD -- Source: Scopus
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  1. Paul J Tempst
    324 Tempst