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Originally published In Press as doi:10.1074/jbc.M007167200 on August 28, 2000

J. Biol. Chem., Vol. 275, Issue 46, 35699-35707, November 17, 2000
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A Role of Basic Residues and the Putative Intercalating Phenylalanine of the HMG-1 Box B in DNA Supercoiling and Binding to Four-way DNA Junctions*

Michal StrosDagger and Eva Muselíková

From the Institute of Biophysics, Academy of Sciences of the Czech Republic, CZ-612 65 Brno, Czech Republic

HMG (high mobility group) 1 is a chromosomal protein with two homologous DNA-binding domains, the HMG boxes A and B. HMG-1, like its individual HMG boxes, can recognize structural distortion of DNA, such as four-way DNA junctions (4WJs), that are very likely to have features common to their natural, yet unknown, cellular binding targets. HMG-1 can also bend/loop DNA and introduce negative supercoils in the presence of topoisomerase I in topologically closed DNAs. Results of our gel shift assays demonstrate that mutation of Arg97 within the extended N-terminal strand of the B domain significantly (>50-fold) decreases affinity of the HMG box for 4WJs and alters the mode of binding without changing the structural specificity for 4WJs. Several basic amino acids of the extended N-terminal strand (Lys96/Arg97) and helix I (Arg110/Lys114) of the B domain participate in DNA binding and supercoiling. The putative intercalating hydrophobic Phe103 of helix I is important for DNA supercoiling but dispensable for binding to supercoiled DNA and 4WJs. We conclude that the B domain of HMG-1 can tolerate substitutions of a number of amino acid residues without abolishing the structure-specific recognition of 4WJs, whereas mutations of most of these residues severely impair the topoisomerase I-mediated DNA supercoiling and change the sign of supercoiling from negative to positive.

* This work was supported by Grant A7004902/1999 from the Internal Grant Agency of the Academy of Sciences of the Czech Republic and Grant 301/99/0691 from the Grant Agency of the Czech Republic (to M. S.).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.

Dagger Recipient of a short-term fellowship from the European Molecular Biology Organization. To whom correspondence should be addressed: Inst. of Biophysics, Academy of Sciences of the Czech Republic, Královopolská 135, CZ-61265 Brno, Czech Republic. Tel.: 420-5-41517183; Fax: 420-5-41211293; E-mail: stros@ibp.cz.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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