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

 Previous Article  |  Next Article 

Molecular and Cellular Biology, April 2006, p. 2791-2802, Vol. 26, No. 7
0270-7306/06/$08.00+0     doi:10.1128/MCB.26.7.2791-2802.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Genome-Wide Relationships between TAF1 and Histone Acetyltransferases in Saccharomyces cerevisiae{dagger}

Melissa Durant and B. Franklin Pugh*

Center for Gene Regulation, Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania 16802

Received 9 November 2005/ Returned for modification 20 December 2005/ Accepted 10 January 2006

Histone acetylation regulates gene expression, yet the functional contributions of the numerous histone acetyltransferases (HATs) to gene expression and their relationships with each other remain largely unexplored. The central role of the putative HAT-containing TAF1 subunit of TFIID in gene expression raises the fundamental question as to what extent, if any, TAF1 contributes to acetylation in vivo and to what extent it is redundant with other HATs. Our findings herein do not support the basic tenet that TAF1 is a major HAT in Saccharomyces cerevisiae, nor do we find that TAF1 is functionally redundant with other HATs, including Gcn5, Elp3, Hat1, Hpa2, Sas3, and Esa1, which is in contrast to previous conclusions regarding Gcn5. Our findings do reveal that of these HATs, only Gcn5 and Esa1 contribute substantially to gene expression genome wide. Interestingly, histone acetylation at promoter regions throughout the genome does not require TAF1 or RNA polymerase II, indicating that most acetylation is likely to precede transcription and not depend upon it. TAF1 function has been linked to Bdf1, which binds TFIID and acetylated histone H4 tails, but no linkage between TAF1 and the H4 HAT Esa1 has been established. Here, we present evidence for such a linkage through Bdf1.


* Corresponding author. Mailing address: 452 North Frear Laboratory, Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, PA 16802. Phone: (814) 863-8252. Fax: (814) 863-8595. E-mail: bfp2{at}psu.edu.

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


Molecular and Cellular Biology, April 2006, p. 2791-2802, Vol. 26, No. 7
0022-538X/06/$08.00+0     doi:10.1128/MCB.26.7.2791-2802.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.




This article has been cited by other articles:

  • Ginsburg, D. S., Govind, C. K., Hinnebusch, A. G. (2009). NuA4 Lysine Acetyltransferase Esa1 Is Targeted to Coding Regions and Stimulates Transcription Elongation with Gcn5. Mol. Cell. Biol. 29: 6473-6487 [Abstract] [Full Text]  
  • Friis, R. M. N., Wu, B. P., Reinke, S. N., Hockman, D. J., Sykes, B. D., Schultz, M. C. (2009). A glycolytic burst drives glucose induction of global histone acetylation by picNuA4 and SAGA. Nucleic Acids Res 37: 3969-3980 [Abstract] [Full Text]  
  • Chakraborty, T., Perlot, T., Subrahmanyam, R., Jani, A., Goff, P. H., Zhang, Y., Ivanova, I., Alt, F. W., Sen, R. (2009). A 220-nucleotide deletion of the intronic enhancer reveals an epigenetic hierarchy in immunoglobulin heavy chain locus activation. JEM 206: 1019-1027 [Abstract] [Full Text]  
  • Jin, Y., Rodriguez, A. M., Wyrick, J. J. (2009). Genetic and Genomewide Analysis of Simultaneous Mutations in Acetylated and Methylated Lysine Residues in Histone H3 in Saccharomyces cerevisiae. Genetics 181: 461-472 [Abstract] [Full Text]  
  • 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]  
  • Kunoh, T., Habu, T., Matsumoto, T. (2008). Involvement of fission yeast Clr6-HDAC in regulation of the checkpoint kinase Cds1. Nucleic Acids Res 36: 3311-3319 [Abstract] [Full Text]  
  • Gomez, E. B., Nugent, R. L., Laria, S., Forsburg, S. L. (2008). Schizosaccharomyces pombe Histone Acetyltransferase Mst1 (KAT5) Is an Essential Protein Required for Damage Response and Chromosome Segregation. Genetics 179: 757-771 [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]  
  • Decker, P. V., Yu, D. Y., Iizuka, M., Qiu, Q., Smith, M. M. (2008). Catalytic-Site Mutations in the MYST Family Histone Acetyltransferase Esa1. Genetics 178: 1209-1220 [Abstract] [Full Text]  
  • Durant, M., Pugh, B. F. (2007). NuA4-Directed Chromatin Transactions throughout the Saccharomyces cerevisiae Genome. Mol. Cell. Biol. 27: 5327-5335 [Abstract] [Full Text]  
  • Garbett, K. A., Tripathi, M. K., Cencki, B., Layer, J. H., Weil, P. A. (2007). Yeast TFIID Serves as a Coactivator for Rap1p by Direct Protein-Protein Interaction. Mol. Cell. Biol. 27: 297-311 [Abstract] [Full Text]  
  • Verdone, L., Agricola, E., Caserta, M., Di Mauro, E. (2006). Histone acetylation in gene regulation. Brief Funct Genomic Proteomic 5: 209-221 [Abstract] [Full Text]