H-NS forms a superhelical protein scaffold for DNA condensation

Stefan Arold, Paul G. Leonard, Gary N. Parkinson, John E. Ladbury

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123 Scopus citations


The histone-like nucleoid structuring (H-NS) protein plays a fundamental role in DNA condensation and is a key regulator of enterobacterial gene expression in response to changes in osmolarity, pH, and temperature. The protein is capable of high-order self-association via interactions of its oligomerization domain. Using crystallography, we have solved the structure of this complete domain in an oligomerized state. The observed superhelical structure establishes a mechanism for the self-association of H-NS via both an N-terminal antiparallel coiled-coil and a second, hitherto unidentified, helix-turn-helix dimerization interface at the C-terminal end of the oligomerization domain. The helical scaffold suggests the formation of a H-NS:plectonemic DNA nucleoprotein complex that is capable of explaining published biophysical and functional data, and establishes a unifying structural basis for coordinating the DNA packaging and transcription repression functions of H-NS.

Original languageEnglish (US)
Pages (from-to)15728-15732
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Issue number36
StatePublished - Sep 7 2010


  • Chromatin
  • DNA binding
  • Nucleoid
  • Supercoil
  • Transcriptional regulation

ASJC Scopus subject areas

  • General

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