Site-Specific Acetylation by p300 or CREB Binding Protein Regulates Erythroid Kruppel-Like Factor Transcriptional Activity via Its Interaction with the SWI-SNF Complex

doi:10.1128/MCB.21.7.2413-2422.2001

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Molecular and Cellular Biology, April 2001, p. 2413-2422, Vol. 21, No. 7
0270-7306/01/$04.00+0 DOI: 10.1128/MCB.21.7.2413-2422.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Site-Specific Acetylation by p300 or CREB Binding Protein Regulates Erythroid Krüppel-Like Factor Transcriptional Activity via Its Interaction with the SWI-SNF Complex

Wenjun Zhang,¹ Shilpa Kadam,² Beverly M. Emerson,² and James J. Bieker¹^,^*

Department of Biochemistry and Molecular Biology, Mount Sinai School of Medicine, New York, NY 10029,¹ and Regulatory Biology Laboratory, Salk Institute for Biological Studies, La Jolla, California 92037²

Received 24 October 2000/Returned for modification 28 November 2000/Accepted 3 January 2001

Recruitment of modifiers and remodelers to specific DNA sites within chromatin plays a critical role in controlling gene expression.The study of globin gene regulation provides a convergence pointwithin which to address these issues in the context of tissue-specificand developmentally regulated expression. In this regard, erythroidKrüppel-like factor (EKLF) is critical. EKLF is a red cell-specificactivator whose presence is crucial for establishment of the correctchromatin structure and high-level transcriptional induction ofadult $beta$ -globin. We now find, by metabolic labeling-immunoprecipitationexperiments, that EKLF is acetylated in the erythroid cell. EKLFresidues acetylated by CREB binding protein (CBP) in vitro mapto Lys-288 in its transactivation domain and Lys-302 in its zincfinger domain. Although site-specific DNA binding by EKLF is unaffectedby the acetylation status of either of these lysines, directedmutagenesis of Lys-288 (but not Lys-302) decreases the abilityof EKLF to transactivate the $beta$ -globin promoter in vivo and rendersit unable to be superactivated by coexpressed p300 or CBP. Inaddition, the acetyltransferase function of CBP or p300 is requiredfor superactivation of wild-type EKLF. Finally, acetylated EKLFhas a higher affinity for the SWI-SNF chromatin remodeling complexand is a more potent transcriptional activator of chromatin-assembledtemplates in vitro. These results demonstrate that the acetylationstatus of EKLF is critical for its optimal activity and suggesta mechanism by which EKLF acts as an integrator of remodelingand transcriptional components to alter chromatin structure andinduce adult $beta$ -globin expression within the $beta$ -like globincluster.

^* Corresponding author. Mailing address: Mount Sinai School of Medicine, Department of Biochemistry and Molecular Biology, Box1020, One Gustave L. Levy Pl., New York, NY 10029. Phone: (212)241-4143. Fax: (212) 860-9279. E-mail: james.bieker{at}mssm.edu.

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