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3-Å resolution structure of a protein with histone-like properties in prokaryotes

Nature volume 310, pages 376–381 (1984)Cite this article

Abstract

The 3-Å structure of DNA-binding protein II, which exhibits histone-like properties in bacteria, has been determined. The molecule is dimeric and appears to bind to the phosphate backbone of DNA through two symmetry-related arms. A mechanism by which the protein induces DNA supercoiling is proposed.

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Author information

Author notes

  1. Isao Tanaka

    Present address: Department of Applied Chemistry, Faculty of Engineering, Nagoya University, Chikusa, Nagoya, 464, Japan

  2. Stephen W. White

    Present address: Biology Department, Brookhaven National Laboratory, Upton, Long Island, New York, 11973, USA

  3. Keith S. Wilson

    Present address: Department of Physics, University of York, Heslington, YO1 5DD, UK

Authors and Affiliations

  1. Max-Planck-Institut für Molekulare Genetik, Abteilung Wittmann, D-1000, Berlin (Dahlem), 33, FRG

    Isao Tanaka, Krzysztof Appelt, Jan Dijk, Stephen W. White & Keith S. Wilson

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  1. Isao Tanaka
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  2. Krzysztof Appelt
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  3. Jan Dijk
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  4. Stephen W. White
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  5. Keith S. Wilson
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Tanaka, I., Appelt, K., Dijk, J. et al. 3-Å resolution structure of a protein with histone-like properties in prokaryotes. Nature 310, 376–381 (1984). https://doi.org/10.1038/310376a0

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