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Molecular and Cellular Biology, October 1999, p. 6621-6631, Vol. 19, No. 10
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

The ADA Complex Is a Distinct Histone Acetyltransferase Complex in Saccharomyces cerevisiae

Anton Eberharter,1,dagger David E. Sterner,2 David Schieltz,3 Ahmed Hassan,1 John R. Yates III,3 Shelley L. Berger,2 and Jerry L. Workman1,*

Howard Hughes Medical Institute and Department of Biochemistry and Molecular Biology, Pennsylvania State University, University Park, Pennsylvania 16802-45001; The Wistar Institute, Philadelphia, Pennsylvania 191042; and Department of Molecular Biotechnology, University of Washington Health Science Center, Seattle, Washington 98195-77303

Received 21 April 1999/Returned for modification 21 May 1999/Accepted 29 June 1999

We have identified two Gcn5-dependent histone acetyltransferase (HAT) complexes from Saccharomyces cerevisiae, the 0.8-MDa ADA complex and the 1.8-MDa SAGA complex. The SAGA (Spt-Ada-Gcn5-acetyltransferase) complex contains several subunits which also function as part of other protein complexes, including a subset of TATA box binding protein-associated factors (TAFIIs) and Tra1. These observations raise the question of whether the 0.8-MDa ADA complex is a subcomplex of SAGA or whether it is a distinct HAT complex that also shares subunits with SAGA. To address this issue, we sought to determine if the ADA complex contained subunits that are not present in the SAGA complex. In this study, we report the purification of the ADA complex over 10 chromatographic steps. By a combination of mass spectrometry analysis and immunoblotting, we demonstrate that the adapter proteins Ada2, Ada3, and Gcn5 are indeed integral components of ADA. Furthermore, we identify the product of the S. cerevisiae gene YOR023C as a novel subunit of the ADA complex and name it Ahc1 for ADA HAT complex component 1. Biochemical functions of YOR023C have not been reported. However, AHC1 in high copy numbers suppresses the cold sensitivity caused by particular mutations in HTA1 (I. Pinto and F. Winston, personal communication), which encodes histone H2A (J. N. Hirschhorn et al., Mol. Cell. Biol. 15:1999-2009, 1995). Deletion of AHC1 disrupted the integrity of the ADA complex but did not affect SAGA or give rise to classic Ada- phenotypes. These results indicate that Gcn5, Ada2, and Ada3 function as part of a unique HAT complex (ADA) and represent shared subunits between this complex and SAGA.

* Corresponding author. Mailing address: Howard Hughes Medical Institute, Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania 16802-4500. Phone: (814) 863-8256. Fax: (814) 863-0099. E-mail: jlw10{at}psu.edu.

dagger Present address: Department of Molecular Biology, Adolf-Butenardt-Institute, 80336 Munich, Germany.

Molecular and Cellular Biology, October 1999, p. 6621-6631, Vol. 19, No. 10
0270-7306/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.


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