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Molecular and Cellular Biology, May 2002, p. 2974-2983, Vol. 22, No. 9
0270-7306/02/$04.00+0     DOI: 10.1128/MCB.22.9.2974-2983.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Dual Roles of p300 in Chromatin Assembly and Transcriptional Activation in Cooperation with Nucleosome Assembly Protein 1 In Vitro

Hiroshi Asahara,1,2 Sophie Tartare-Deckert,1,3,{dagger} Takeya Nakagawa,4 Tsuyoshi Ikehara,4 Fumiko Hirose,5 Tony Hunter,3 Takashi Ito,4* and Marc Montminy1*

Peptide Biology Laboratory,1 Molecular and Cell Biology Laboratory, Salk Institute for Biological Studies, La Jolla, California 92037,3 Division of Gene Structure and Function, Saitama Medical School Research Center for Genomic Medicine, Morohongo Moroyama, Iruma, Saitama 350-0495,4 Laboratory of Cell Biology, Aichi Cancer Center Research Institute, Chikusa-ku, Nagoya 464-8681,5 PRESTO, Japan Science and Technology Corporation, Kawaguchi 332-0012, Japan2

Received 2 July 2001/ Returned for modification 26 October 2001/ Accepted 29 January 2002

In a yeast two-hybrid screen to identify proteins that bind to the KIX domain of the coactivator p300, we obtained cDNAs encoding nucleosome assembly protein 1 (NAP-1), a 60-kDa histone H2A-H2B shuttling protein that promotes histone deposition. p300 associates preferentially with the H2A-H2B-bound form of NAP-1 rather than with the unbound form of NAP-1. Formation of NAP-1-p300 complexes was found to increase during S phase, suggesting a potential role for p300 in chromatin assembly. In micrococcal nuclease and supercoiling assays, addition of p300 promoted efficient chromatin assembly in vitro in conjunction with NAP-1 and ATP-utilizing chromatin assembly and remodeling factor; this effect was dependent in part on the intrinsic histone acetyltransferase activity of p300. Surprisingly, NAP-1 potently inhibited acetylation of core histones by p300, suggesting that efficient assembly requires acetylation of either NAP-1 or p300 itself. As p300 acted cooperatively with NAP-1 in stimulating transcription from a chromatin template in vitro, our results suggest a dual role of NAP-1-p300 complexes in promoting chromatin assembly and transcriptional activation.

* Corresponding author. Present address for Takashi Ito: Division of Gene Structure and Function, Saitama Medical School Research Center for Genomic Medicine, 1397-1 Inariyama, Yamane, Hidaka, Saitama 350-1241, Japan. Phone: 81-429-85-7343 or -7339. Fax: 81-429-85-7347. E-mail: tito{at}saitama-med.ac.jp.

* Corresponding author. Mailing address for Marc Montminy: Salk Institute, 10010 N. Torrey Pines Rd., La Jolla, CA 92037. Phone: (858) 453-4100, ext. 1394. Fax: (858) 625-9045. E-mail: montminy{at}salk.edu.

{dagger} Present address: INSERM Unité 145, IFR 50, Faculté de Médecine, Nice 06107, France.

Molecular and Cellular Biology, May 2002, p. 2974-2983, Vol. 22, No. 9
0022-538X/02/$04.00+0     DOI: 10.1128/MCB.22.9.2974-2983.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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