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

J. Richard G. Pöhler, David G. Norman, Janice Bramham, Marco E. Bianchi, David M.J. Lilley (Lead / Corresponding author)

    Research output: Contribution to journalArticlepeer-review

    103 Citations (Scopus)

    Abstract

    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.

    Original languageEnglish
    Pages (from-to)817-826
    Number of pages10
    JournalEMBO Journal
    Volume17
    Issue number3
    DOIs
    Publication statusPublished - 2 Feb 1998

    Keywords

    • DNA-protein interaction
    • HMG1
    • Holliday junction
    • SRY
    • UBF

    ASJC Scopus subject areas

    • General Neuroscience
    • Molecular Biology
    • General Biochemistry,Genetics and Molecular Biology
    • General Immunology and Microbiology

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