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, August 2007, p. 5327-5335, Vol. 27, No. 15
0270-7306/07/$08.00+0     doi:10.1128/MCB.00468-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

NuA4-Directed Chromatin Transactions throughout the Saccharomyces cerevisiae Genome{triangledown} ,{dagger}

Melissa Durant{ddagger} and B. Franklin Pugh*

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

Received 19 March 2007/ Returned for modification 19 April 2007/ Accepted 17 May 2007

Two of the major histone acetyltransferases in Saccharomyces cerevisiae are NuA4 and SAGA, which acetylate histones H4 and H3, respectively. Acetylated H3 and H4 tails have been implicated in binding bromodomain proteins, including Bdf1. Bdf1 interacts with the general transcription factor TFIID, which might promote preinitiation complex (PIC) assembly. Bdf1 also interacts with the SWR complex (SWR-C). SWR-C is responsible for the deposition of the histone H2A variant H2A.Z. The placement of these interactions into a connected pathway of PIC assembly has not been fully established. Moreover, it is not known how widespread and how variable such a pathway might be on a genomic scale. Here we provide genomic evidence for S. cerevisiae that PIC assembly (TFIID occupancy) and chromatin remodeling (SWR-C and H2A.Z occupancy) are linked in large part to NuA4-directed H4 acetylation and subsequent Bdf1 binding, rather than through SAGA-directed H3 acetylation. Bdf1 and its homolog Bdf2 tend to have distinct locations in the genome. However, the deletion of BDF1 leads to the accumulation of Bdf2 at Bdf1-vacated sites. Thus, while Bdf1 and Bdf2 are at least partially redundant in function, their functions in the genome are geographically distinct.

* 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) 863-7024. E-mail: bfp2{at}psu.edu

{triangledown} Published ahead of print on 25 May 2007.

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

{ddagger} Present address: Laboratory of Molecular Genetics, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892.

Molecular and Cellular Biology, August 2007, p. 5327-5335, Vol. 27, No. 15
0270-7306/07/$08.00+0     doi:10.1128/MCB.00468-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Choi, J., Heo, K., An, W. (2009). Cooperative action of TIP48 and TIP49 in H2A.Z exchange catalyzed by acetylation of nucleosomal H2A. Nucleic Acids Res 37: 5993-6007 [Abstract] [Full Text]  
  • Wu, W.-H., Wu, C.-H., Ladurner, A., Mizuguchi, G., Wei, D., Xiao, H., Luk, E., Ranjan, A., Wu, C. (2009). N Terminus of Swr1 Binds to Histone H2AZ and Provides a Platform for Subunit Assembly in the Chromatin Remodeling Complex. J. Biol. Chem. 284: 6200-6207 [Abstract] [Full Text]  
  • Arimbasseri, A. G., Bhargava, P. (2008). Chromatin Structure and Expression of a Gene Transcribed by RNA Polymerase III Are Independent of H2A.Z Deposition. Mol. Cell. Biol. 28: 2598-2607 [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]  
  • 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]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»