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Molecular and Cellular Biology, March 2004, p. 2364-2372, Vol. 24, No. 6
0270-7306/04/$08.00+0     DOI: 10.1128/MCB.24.6.2364-2372.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

In Vitro Targeting Reveals Intrinsic Histone Tail Specificity of the Sin3/Histone Deacetylase and N-CoR/SMRT Corepressor Complexes

Michiel Vermeulen,1 Michael J. Carrozza,2,{dagger} Edwin Lasonder,1 Jerry L. Workman,2,{dagger} Colin Logie,1 and Hendrik G. Stunnenberg1*

Department of Molecular Biology, University of Nijmegen, 6500 HB Nijmegen, The Netherlands,1 Howard Hughes Medical Institute, Department of Biochemistry and Molecular Biology, Pennsylvania State University, University Park, Pennsylvania 168022

Received 25 August 2003/ Returned for modification 27 October 2003/ Accepted 15 December 2003

The histone code is among others established via differential acetylation catalyzed by histone acetyltransferases (HATs) and histone deacetylases (HDACs). To unambiguously determine the histone tail specificity of HDAC-containing complexes, we have established an in vitro system consisting of nucleosomal templates reconstituted with hyperacetylated histones or recombinant histones followed by acetylation with native SAGA or NuA4. Selective targeting of the mammalian Sin3/HDAC and N-CoR/SMRT corepressor complexes by using specific chimeric repressors created a near physiological setting to assess their histone tail specificity. Recruitment of the Sin3/HDAC complex to nucleosomal templates preacetylated with SAGA or NuA4 resulted in deacetylation of histones H3 and H4, whereas recruitment of N-CoR/SMRT resulted in deacetylation of histone H3 only. These results provide solid evidence that HDAC-containing complexes display distinct, intrinsic histone tail specificities and hence may function differently to regulate chromatin structure and transcription.

* Corresponding author. Mailing address: Department of Molecular Biology, NCMLS 191, University of Nijmegen, P.O. Box 9101, 6500 HB Nijmegen, The Netherlands. Phone: 31-24-3610524. Fax: 31-24-3610520. E-mail: h.stunnenberg{at}ncmls.kun.nl.

{dagger} Present address: Stowers Institute for Medical Research, Kansas City, MO 64110.

Molecular and Cellular Biology, March 2004, p. 2364-2372, Vol. 24, No. 6
0022-538X/04/$08.00+0     DOI: 10.1128/MCB.24.6.2364-2372.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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