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J. Biol. Chem., Vol. 265, Issue 15, 8573-8582, May, 1990
R Reeves and MS Nissen
We have determined the domains of the mammalian high mobility group (HMG)I
chromosomal proteins necessary and sufficient for binding to the narrow
minor groove of stretches of A.T-rich DNA. Three highly conserved regions
within each of the known HMG-I proteins is closely related to the consensus
sequence T-P-K-R-P-R-G-R-P-K-K. A synthetic oligopeptide corresponding to
this consensus "binding domain" (BD) sequence specifically binds to
substrate DNA in a manner similar to the intact HMG-I proteins. Molecular
Corey-Pauling-Koltun model building and computer simulations employing
energy minimization programs to predict structure suggest that the
consensus BD peptide has a secondary structure similar to the antitumor and
antiviral drugs netropsin and distamycin and to the dye Hoechst 33258. In
vitro these ligands, which also preferentially bind to A.T-rich DNA, have
been demonstrated to effectively compete with both the BD peptide and the
HMG-I proteins for DNA binding. The BD peptide also contains novel
structural features such as a predicted Asx bend or "hook" at its
amino-terminal end and laterally projecting cationic Arg/Lys side chains or
"bristles" which may contribute to the binding properties of the HMG-I
proteins. The predicted BD peptide structure, which we refer to as the
"A.T-hook," represents a previously undescribed DNA-binding motif capable
of binding to the minor groove of stretches of A.T base pairs.
The A.T-DNA-binding domain of mammalian high mobility group I chromosomal proteins. A novel peptide motif for recognizing DNA structure
Department of Biochemistry/Biophysics, Washington State University, Pullman 99164.
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