This Article Full Text Full Text (PDF) Supplemental material Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Zhang, H. Articles by Cairns, B. R. Search for Related Content PubMed PubMed Citation Articles by Zhang, H. Articles by Cairns, B. R.

 Previous Article  |  Next Article 

Molecular and Cellular Biology, November 2004, p. 9424-9436, Vol. 24, No. 21
0270-7306/04/$08.00+0     DOI: 10.1128/MCB.24.21.9424-9436.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

The Yaf9 Component of the SWR1 and NuA4 Complexes Is Required for Proper Gene Expression, Histone H4 Acetylation, and Htz1 Replacement near Telomeres

Haiying Zhang,^1,2, Daniel O. Richardson,^1,2, Douglas N. Roberts,^1,2 Rhea Utley,³ Hediye Erdjument-Bromage,⁴ Paul Tempst,⁴ Jacques Côté,³ and Bradley R. Cairns^1,2*

Howard Hughes Medical Institute,¹ Department of Oncological Sciences, School of Medicine, University of Utah, Salt Lake City, Utah,² Molecular Biology Program, Memorial Sloan-Kettering Cancer Center, New York, New York,⁴ Cancer Research Center, Laval University, Quebec City, Quebec, Canada³

Received 12 March 2004/ Returned for modification 9 April 2004/ Accepted 7 August 2004

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 yaf9 taf14 sas5 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, yaf9 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 yaf9 and htz1 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.

Supplemental material for this article may be found at http://mcb.asm.org/.

H.Z. and D.O.R. contributed equally to this work.

This article has been cited by other articles:

• Lin, Y.-y., Qi, Y., Lu, J.-y., Pan, X., Yuan, D. S., Zhao, Y., Bader, J. S., Boeke, J. D. (2008). A comprehensive synthetic genetic interaction network governing yeast histone acetylation and deacetylation. Genes Dev. 22: 2062-2074 [Abstract] [Full Text]  
• Mitchell, L., Lambert, J.-P., Gerdes, M., Al-Madhoun, A. S., Skerjanc, I. S., Figeys, D., Baetz, K. (2008). Functional Dissection of the NuA4 Histone Acetyltransferase Reveals Its Role as a Genetic Hub and that Eaf1 Is Essential for Complex Integrity. Mol. Cell. Biol. 28: 2244-2256 [Abstract] [Full Text]  
• Auger, A., Galarneau, L., Altaf, M., Nourani, A., Doyon, Y., Utley, R. T., Cronier, D., Allard, S., Cote, J. (2008). Eaf1 Is the Platform for NuA4 Molecular Assembly That Evolutionarily Links Chromatin Acetylation to ATP-Dependent Exchange of Histone H2A Variants. Mol. Cell. Biol. 28: 2257-2270 [Abstract] [Full Text]  
• Hershman, S. G., Chen, Q., Lee, J. Y., Kozak, M. L., Yue, P., Wang, L.-S., Johnson, F. B. (2008). Genomic distribution and functional analyses of potential G-quadruplex-forming sequences in Saccharomyces cerevisiae. Nucleic Acids Res 36: 144-156 [Abstract] [Full Text]  
• Gordon, M., Holt, D. G., Panigrahi, A., Wilhelm, B. T., Erdjument-Bromage, H., Tempst, P., Bahler, J., Cairns, B. R. (2007). Genome-Wide Dynamics of SAPHIRE, an Essential Complex for Gene Activation and Chromatin Boundaries. Mol. Cell. Biol. 27: 4058-4069 [Abstract] [Full Text]  
• Ogiwara, H., Ui, A., Kawashima, S., Kugou, K., Onoda, F., Iwahashi, H., Harata, M., Ohta, K., Enomoto, T., Seki, M. (2007). Actin-related protein Arp4 functions in kinetochore assembly. Nucleic Acids Res 35: 3109-3117 [Abstract] [Full Text]  
• Shia, W.-J., Li, B., Workman, J. L. (2006). SAS-mediated acetylation of histone H4 Lys 16 is required for H2A.Z incorporation at subtelomeric regions in Saccharomyces cerevisiae. Genes Dev. 20: 2507-2512 [Abstract] [Full Text]  
• Lindstrom, K. C., Vary, J. C. Jr., Parthun, M. R., Delrow, J., Tsukiyama, T. (2006). Isw1 Functions in Parallel with the NuA4 and Swr1 Complexes in Stress-Induced Gene Repression.. Mol. Cell. Biol. 26: 6117-6129 [Abstract] [Full Text]  
• Park, J. H., Roeder, R. G. (2006). GAS41 Is Required for Repression of the p53 Tumor Suppressor Pathway during Normal Cellular Proliferation.. Mol. Cell. Biol. 26: 4006-4016 [Abstract] [Full Text]  
• Babiarz, J. E., Halley, J. E., Rine, J. (2006). Telomeric heterochromatin boundaries require NuA4-dependent acetylation of histone variant H2A.Z in Saccharomy cescerevisiae.. Genes Dev. 20: 700-710 [Abstract] [Full Text]  
• Li, B., Pattenden, S. G., Lee, D., Gutierrez, J., Chen, J., Seidel, C., Gerton, J., Workman, J. L. (2005). Preferential occupancy of histone variant H2AZ at inactive promoters influences local histone modifications and chromatin remodeling. Proc. Natl. Acad. Sci. USA 102: 18385-18390 [Abstract] [Full Text]  
• Bruce, K., Myers, F. A., Mantouvalou, E., Lefevre, P., Greaves, I., Bonifer, C., Tremethick, D. J., Thorne, A. W., Crane-Robinson, C. (2005). The replacement histone H2A.Z in a hyperacetylated form is a feature of active genes in the chicken. Nucleic Acids Res 33: 5633-5639 [Abstract] [Full Text]  
• Shia, W.-J., Osada, S., Florens, L., Swanson, S. K., Washburn, M. P., Workman, J. L. (2005). Characterization of the Yeast Trimeric-SAS Acetyltransferase Complex. J. Biol. Chem. 280: 11987-11994 [Abstract] [Full Text]  
• Kamakaka, R. T., Biggins, S. (2005). Histone variants: deviants?. Genes Dev. 19: 295-316 [Abstract] [Full Text]