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Molecular and Cellular Biology, May 2003, p. 3468-3476, Vol. 23, No. 10
0270-7306/03/$08.00+0     DOI: 10.1128/MCB.23.10.3468-3476.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Multiple Mechanistically Distinct Functions of SAGA at the PHO5 Promoter

Slobodan Barbaric,1 Hans Reinke,2 and Wolfram Hörz2*

Laboratory of Biochemistry, Faculty of Food Technology and Biotechnology, University of Zagreb, 10000 Zagreb, Croatia,1 Adolf-Butenandt-Institut Molekularbiologie, Universität München, 80336 Münich, Germany2

Received 14 November 2002/ Returned for modification 17 December 2002/ Accepted 20 February 2003

Our previous studies have shown that the rate of chromatin remodeling and consequently the rate of PHO5 activation are strongly decreased in the absence of Gcn5 histone acetyltransferase activity. Using chromatin immunoprecipitation, we demonstrate that SAGA is physically recruited to the PHO5 promoter. Recruitment is dependent on the specific activator Pho4 and occurs only under inducing conditions. Spt3, another subunit of SAGA, also plays a role in PHO5 activation but has a function that is completely different from that of Gcn5. An SPT3 deletion severely compromises the PHO5 promoter and reduces the extent of transcriptional activation by diminishing the binding of the TATA binding protein to the promoter without, however, affecting the rate or the extent of chromatin remodeling. A gcn5 spt3 double mutant shows a synthetic phenotype almost as severe as that observed for an spt7 or spt20 mutant. The latter two mutations are known to prevent the assembly of the complex and consequently lead to the loss of all SAGA functions. The absence of the Ada2 subunit causes a strong delay in chromatin remodeling and promoter activation that closely resembles the delay observed in the absence of Gcn5. A deletion of only the Ada2 SANT domain has exactly the same effect, strongly suggesting that Ada2 controls Gcn5 activity by virtue of its SANT domain. Finally, the Gcn5 bromodomain also contributes to but is not essential for Gcn5 function at the PHO5 promoter. Taken together, the results provide a detailed and differentiated description of the role of SAGA as a coactivator at the PHO5 promoter.

* Corresponding author. Mailing address: Adolf-Butenandt-Institut Molekularbiologie, Universität München, Schillerstr. 44, 80336 Münich, Germany. Phone: 49 89-5996 420. Fax: 49 89-5996 440. E-mail: Hoerz{at}bio.med.uni-muenchen.de.

Molecular and Cellular Biology, May 2003, p. 3468-3476, Vol. 23, No. 10
0022-538X/03/$08.00+0     DOI: 10.1128/MCB.23.10.3468-3476.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



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