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Molecular and Cellular Biology, February 2005, p. 958-968, Vol. 25, No. 3
0270-7306/05/$08.00+0     doi:10.1128/MCB.25.3.958-968.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Common Effects of Acidic Activators on Large-Scale Chromatin Structure and Transcription

Anne E. Carpenter,{dagger} Sevinci Memedula, Matthew J. Plutz, and Andrew S. Belmont*

Department of Cell and Structural Biology, University of Illinois at Urbana-Champaign, Urbana, Illinois

Received 23 July 2004/ Returned for modification 11 August 2004/ Accepted 5 November 2004

Large-scale chromatin decondensation has been observed after the targeting of certain acidic activators to heterochromatic chromatin domains. Acidic activators are often modular, with two or more separable transcriptional activation domains. Whether these smaller regions are sufficient for all functions of the activators has not been demonstrated. We adapted an inducible heterodimerization system to allow systematic dissection of the function of acidic activators, individual subdomains within these activators, and short acidic-hydrophobic peptide motifs within these subdomains. Here, we demonstrate that large-scale chromatin decondensation activity is a general property of acidic activators. Moreover, this activity maps to the same acidic activator subdomains and acidic-hydrophobic peptide motifs that are responsible for transcriptional activation. Two copies of a mutant peptide motif of VP16 (viral protein 16) possess large-scale chromatin decondensation activity but minimal transcriptional activity, and a synthetic acidic-hydrophobic peptide motif had large-scale chromatin decondensation activity comparable to the strongest full-length acidic activator but no transcriptional activity. Therefore, the general property of large-scale chromatin decondensation shared by most acidic activators is not simply a direct result of transcription per se but is most likely the result of the concerted action of coactivator proteins recruited by the activators' short acidic-hydrophobic peptide motifs.

* Corresponding author. Mailing address: B107 CLSL, 601 S. Goodwin Ave., Urbana, IL 61801. Phone: (217) 244-2311. Fax: (217) 244-1648. E-mail: asbel{at}uiuc.edu.

{dagger} Present address: Whitehead Institute for Biomedical Research, Cambridge, MA 02142.

Molecular and Cellular Biology, February 2005, p. 958-968, Vol. 25, No. 3
0022-538X/05/$08.00+0     doi:10.1128/MCB.25.3.958-968.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



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