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For successful DNA replication, the unwinding of double-stranded DNA must be accompanied by stabilization and protection of the separated single strands of the DNA. This crucial task is performed by single-strand DNA-binding (SSB) proteins. They bind to the DNA in a sequence-independent manner, which means that the nitrogenous bases of the DNA need not be present in a specific order for binding of SSB proteins to it. The binding of SSB proteins straightens single-stranded DNA (ssDNA) and makes...
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E. coli DNA binding protein HU forms nucleosomelike structure with circular double-stranded DNA.

J Rouvière-Yaniv, M Yaniv, J E Germond

    Cell
    |June 1, 1979
    PubMed
    Summary

    The E coli DNA binding protein HU compacts DNA, introducing superhelical turns and forming bead-like structures. These DNA-HU complexes resemble chromatin, suggesting a role in DNA organization.

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    Area of Science:

    • Molecular Biology
    • Biochemistry
    • Structural Biology

    Background:

    • DNA supercoiling is crucial for genome organization and regulation.
    • Bacterial DNA binding proteins play a role in compacting the bacterial nucleoid.

    Purpose of the Study:

    • To investigate the effect of E. coli DNA binding protein HU on DNA supercoiling and structure.
    • To compare DNA-HU complexes with eukaryotic chromatin structure.

    Main Methods:

    • Agarose gel electrophoresis to measure DNA superhelicity.
    • Electron microscopy to visualize DNA-HU complexes.
    • Crosslinking with glutaraldehyde to stabilize complexes.

    Main Results:

    • HU introduced up to 18 negative superhelical turns in SV40 DNA.
    • Maximal supercoiling density occurred at a HU-DNA mass ratio of 1.
    • DNA-HU complexes formed condensed circular structures with an average of 14 beads per molecule.
    • DNA condensation ratio (2.0-2.5) was similar to that of histone-formed chromatin (2.4).

    Conclusions:

    • E. coli HU protein can significantly supercoil DNA.
    • DNA-HU complexes exhibit structural similarities to eukaryotic chromatin.
    • HU may play a role in organizing bacterial DNA in a manner analogous to histones.