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Molecular and Cellular Biology, February 2006, p. 871-882, Vol. 26, No. 3
0270-7306/06/$08.00+0     doi:10.1128/MCB.26.3.871-882.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Host Cell Factor and an Uncharacterized SANT Domain Protein Are Stable Components of ATAC, a Novel dAda2A/dGcn5-Containing Histone Acetyltransferase Complex in Drosophila

Sebastián Guelman,1,2 Tamaki Suganuma,1 Laurence Florens,1 Selene K. Swanson,1 Cheri L. Kiesecker,1 Thomas Kusch,1 Scott Anderson,3 John R. Yates III,3 Michael P. Washburn,1 Susan M. Abmayr,1 and Jerry L. Workman1*

Stowers Institute for Medical Research, 1000 E. 50th St., Kansas City, Missouri 64110,1 Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania 16802,2 Department of Cell Biology, The Scripps Research Institute, 10550 N. Torrey Pines Rd., La Jolla, California 920373

Received 31 March 2005/ Returned for modification 6 May 2005/ Accepted 4 November 2005

Gcn5 is a conserved histone acetyltransferase (HAT) found in a number of multisubunit complexes from Saccharomyces cerevisiae, mammals, and flies. We previously identified Drosophila melanogaster homologues of the yeast proteins Ada2, Ada3, Spt3, and Tra1 and showed that they associate with dGcn5 to form at least two distinct HAT complexes. There are two different Ada2 homologues in Drosophila named dAda2A and dAda2B. dAda2B functions within the Drosophila version of the SAGA complex (dSAGA). To gain insight into dAda2A function, we sought to identify novel components of the complex containing this protein, ATAC (Ada two A containing) complex. Affinity purification and mass spectrometry revealed that, in addition to dAda3 and dGcn5, host cell factor (dHCF) and a novel SANT domain protein, named Atac1 (ATAC component 1), copurify with this complex. Coimmunoprecipitation experiments confirmed that these proteins associate with dGcn5 and dAda2A, but not with dSAGA-specific components such as dAda2B and dSpt3. Biochemical fractionation revealed that ATAC has an apparent molecular mass of 700 kDa and contains dAda2A, dGcn5, dAda3, dHCF, and Atac1 as stable subunits. Thus, ATAC represents a novel histone acetyltransferase complex that is distinct from previously purified Gcn5/Pcaf-containing complexes from yeast and mammalian cells.

* Corresponding author. Mailing address: Stowers Institute for Medical Research, 1000 E. 50th St., Kansas City, MO 64110. Phone: (816) 926-4312. Fax: (816) 926-4692. E-mail: jlw{at}stowers-institute.org.

Molecular and Cellular Biology, February 2006, p. 871-882, Vol. 26, No. 3
0270-7306/06/$08.00+0     doi:10.1128/MCB.26.3.871-882.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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