HMG box proteins bind to four-way DNA junctions in their open conformation

The HMG box is an 80 amino acid domain found in a variety of eukaryotic chromosomal proteins and transcription factors. Binding to DNA is associated with recognition of structural distortion or manipulation of DNA structure. All the HMG box domains bind to four‐way DNA junctions, which must therefor...

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Bibliographic Details
Published in:The EMBO journal 1998-02, Vol.17 (3), p.817-826
Main Authors: Pöhler, J.Richard G., Norman, David G., Bramham, Janice, Bianchi, Marco E., Lilley, David M.J.
Format: Article
Language:English
Subjects:
Animals
Carrier Proteins - antagonists & inhibitors
Carrier Proteins - genetics
Carrier Proteins - metabolism
DNA - chemistry
DNA - metabolism
DNA-Binding Proteins - antagonists & inhibitors
DNA-Binding Proteins - metabolism
DNA-protein interaction
Gene Expression - genetics
High Mobility Group Proteins - chemistry
High Mobility Group Proteins - genetics
High Mobility Group Proteins - metabolism
HMG1
Holliday junction
Macromolecular Substances
Magnesium - pharmacology
Maltose-Binding Proteins
Molecular Probes
Nucleic Acid Conformation
Protein Conformation
Protein Structure, Tertiary
Rats
Recombinant Fusion Proteins - genetics
Recombinant Fusion Proteins - metabolism
SRY
Thymine - analysis
Thymine - chemistry
UBF
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Summary:The HMG box is an 80 amino acid domain found in a variety of eukaryotic chromosomal proteins and transcription factors. Binding to DNA is associated with recognition of structural distortion or manipulation of DNA structure. All the HMG box domains bind to four‐way DNA junctions, which must therefore present some feature that is common to the binding targets of this wide variety of proteins. Since the four‐way junction can itself adopt a variety of structures depending upon conditions, it is important to determine in which form it exists in complexes with HMG boxes. We find that a single HMG box domain is bound exclusively to the open square form of the junction and that conditions that stabilize the stacked X structure significantly lower affinity for the HMG box. We suggest that the HMG domain binds to one arm of the junction in the minor groove at the point of strand exchange and we present a model for the structure of the complex.
ISSN:0261-4189
1460-2075
1460-2075
DOI:10.1093/emboj/17.3.817