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Molecular and Cellular Biology, June 2002, p. 3698-3706, Vol. 22, No. 11
0270-7306/02/$04.00+0     DOI: 10.1128/MCB.22.11.3698-3706.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Ligand-Selective Potentiation of Rat Mineralocorticoid Receptor Activation Function 1 by a CBP-Containing Histone Acetyltransferase Complex

Hirochika Kitagawa,1,2 Junn Yanagisawa,1,3 Hiroaki Fuse,4 Satoko Ogawa,1 Yoshiko Yogiashi,1,3 Atsuro Okuno,5 Hiromichi Nagasawa,5 Toshihiro Nakajima,6 Toshio Matsumoto,2 and Shigeaki Kato1,3*

Institute of Molecular and Cellular Biosciences,1 Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, University of Tokyo, Bunkyo-ku,5 Pharmacological Research Department, Teikoku Hormone Manufacturing Company, Ltd., Tokyo,4 First Department of Internal Medicine, University of Tokushima School of Medicine, Tokushima,2 CREST, Japan Science and Technology, Kawaguchi, Saitama,3 Institute of Medical Science, St. Marianna University School of Medicine, Miyamae-ku, Kawasaki, Japan6

Received 16 November 2001/ Returned for modification 31 January 2002/ Accepted 21 February 2002

The rat mineralocorticoid receptor (MR) has two activation functions in distinct regions of the A/B domain, designated activation function 1a (AF-1a; amino acids 1 to 169) and AF-1b (amino acids 451 to 600). Since the p160 family protein TIF2, a known component of the AF-2 coactivator complex, potentiates the transactivation function of AF-1b but not that of AF-1a, it is likely that some other, novel protein complex interacts with the AF-1a region. Therefore, we attempted to identify such coactivator complexes from HeLa nuclear extracts by biochemical purification using a glutathione S-transferase-MR AF-1a fusion protein. Purified AF-1a region-interacting proteins were found to contain RNA helicase A (RHA) and CBP. Further analysis showed that RHA interacted with the AF-1a region directly and then recruited a complex with histone acetyltransferase (HAT) activity that contained CBP. For full-length MR, aldosterone, but not hydrocortisone, was found to induce the binding of RHA/CBP complexes to the AF-1a region, as well as to allow the cooperative potentiation of MR transcriptional activity by RHA and CBP. In addition, a chromatin immunoprecipitation assay showed that aldosterone-bound MR, but not hydrocortisone-bound MR, recruited RHA/CBP complexes to native MR target gene promoters. Our results suggested that an altered conformation of the A/B region induced by aldosterone, but not hydrocortisone, might determine the accessibility of MR AF-1a to RHA/CBP complexes.

* Corresponding author. Mailing address: Institute of Molecular and Cellular Bioscience, University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-0032, Japan. Phone: 81-3-5841-7891. Fax: 81-3-5841-8477. E-mail: uskato{at}mail.ecc.u-tokyo.ac.jp.

Molecular and Cellular Biology, June 2002, p. 3698-3706, Vol. 22, No. 11
0022-538X/02/$04.00+0     DOI: 10.1128/MCB.22.11.3698-3706.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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