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J Biol Chem, Vol. 273, Issue 32, 20015-20020, August 7, 1998
From the III. Zoologisches Institut-Entwicklungsbiologie,
Universität Göttingen, Humboldtallee 34A, 37073 Göttingen, Germany
The high mobility group proteins I and Y (HMGI/Y)
are abundant components of chromatin. They are thought to derepress
chromatin, affect the assembly and activity of the transcriptional
machinery, and associate with constitutive heterochromatin during
mitosis. HMGI/Y protein molecules contain three potential DNA-binding
motifs (AT-hooks), but the extent of contacts between DNA
and the entire protein has not been determined. We have used a
protein-footprinting procedure to map regions of the
Chironomus HMGI protein molecule that are involved in
contacts with DNA. We find that in the presence of double-stranded DNA
all AT-hook motifs are protected against hydroxyl radical
proteolysis. In contrast, only two motifs were protected in the
presence of four-way junction DNA. Large regions that flank the
AT-hook motifs were found to be strongly protected against
proteolysis in complexes with interferon-
Protein Footprinting Reveals Specific Binding Modes of a High
Mobility Group Protein I to DNAs of Different Conformation
niewski
promoter DNA, suggesting
amino acid residues outside the AT-hooks considerably contribute to DNA binding.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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