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Originally published In Press as doi:10.1074/jbc.M509330200 on December 20, 2005

J. Biol. Chem., Vol. 281, Issue 7, 4523-4531, February 17, 2006
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Snf1p-dependent Spt-Ada-Gcn5-acetyltransferase (SAGA) Recruitment and Chromatin Remodeling Activities on the HXT2 and HXT4 Promoters*Formula

Chris J. C. van Oevelen, Hetty A. A. M. van Teeffelen, Folkert J. van Werven, and H. Th. Marc Timmers1

From the Department of Physiological Chemistry, Division of Biomedical Genetics, University Medical Center Utrecht, Universiteitsweg 100, 3584 CG Utrecht, The Netherlands

We previously showed that the Spt-Ada-Gcn5-acetyltransferase (SAGA) complex is recruited to the activated HXT2 and HXT4 genes and plays a role in the association of TBP-associated factors. Using the HXT2 and HXT4 genes, we now present evidence for a functional link between Snf1p-dependent activation, recruitment of the SAGA complex, histone H3 removal, and H3 acetylation. Recruitment of the SAGA complex is dependent on the release of Ssn6p-Tup1p repression by Snf1p. In addition, we found that the Gcn5p subunit of the SAGA complex preferentially acetylates histone H3K18 on the HXT2 and HXT4 promoters and that Gcn5p activity is required for removal of histone H3 from the HXT4 promoter TATA region. In contrast, histone H3 removal from the HXT2 promoter does not require Gcn5p. In conclusion, although similar protein complexes are involved, induction of HXT2 and HXT4 displays important mechanistic differences.


Received for publication, August 24, 2005 , and in revised form, November 21, 2005.

* This work was supported by The Netherlands Organization for Scientific Research (Grants NWO-MW Pionier 900-98-142 and NWO-ALW MtC 805-47-080) and the European Union (Grant LSHG-CT-2004-502950). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Formula The on-line version of this article (available at http://www.jbc.org) contains supplemental Fig. S1.

1 To whom correspondence should be addressed. Tel.: 31-30-253-8981; Fax: 31-30-253-9035; E-mail: h.t.m.timmers{at}med.uu.nl.


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