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Originally published In Press as doi:10.1074/jbc.M004065200 on October 16, 2000

J. Biol. Chem., Vol. 276, Issue 3, 1984-1992, January 19, 2001
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Distinct Organization of DNA Complexes of Various HMGI/Y Family Proteins and Their Modulation upon Mitotic Phosphorylation*

Agnieszka PiekiełkoDagger §, Alexander DrungDagger , Piere Rogalla, Ralf SchwanbeckDagger , Tomasz Heyduk||, Melanie GerharzDagger , Jörn Bullerdiek, and Jacek R. WisniewskiDagger **

From the Dagger  III. Zoologisches Institut-Entwicklungsbiologie, Universität Göttingen, D-37073 Göttingen, Germany, the  Zentrum für Humangenetik und Genetische Beratung, Universität Bremen, ZHG, D-28359 Bremen, Germany, and the || Edward A. Doisy Department of Biochemistry and Molecular Biology, St. Louis University Medical School, St. Louis, Missouri 63104

High mobility group (HMG) proteins HMGI, HMGY, HMGI-C, and Chironomus HMGI are DNA-binding proteins thought to modulate the assembly and the function of transcriptional complexes. Each of these proteins contains three DNA-binding domains (DBD), properties of which appear to be regulated by phosphorylation. High levels of these proteins are characteristic for rapidly dividing cells in embryonic tissues and tumors. On the basis of their occurrence, specific functions for each of these proteins have been postulated. In this study we demonstrate differences in the nature of contacts of these proteins with promoter region of the interferon-beta gene. We show that HMGI and HMGY interact with this DNA via three DBDs, whereas HMGI-C and Chironomus HMGI bind to this DNA using only two domains. Phosphorylation of HMGY protein by Cdc2 kinase leads to impairing of contacts between the N-terminally located DBD and a single promoter element. The perturbations in the architecture of the protein·DNA complexes involve changes in the degree of unbending of the intrinsically bent IFNbeta promoter. Our results provide first insights into the molecular basis of functional specificity of proteins of the HMGI/Y family and their regulation by phosphorylation.

* This work was supported by Grants Wi-1210/2-1 and Wi-1210/3-1 (to J. R. W.) from the Deutsche Forschungsgemeinschaft.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ Present affiliation: Inst. of Biochemistry, Warsaw University, 02-096 Warszawa, Poland.

** To whom correspondence should be addressed. Fax: 49-551-395416; E-mail: jwisnie@gwdg.de.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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