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H-NS forms a superhelical protein scaffold for DNA condensation.


ABSTRACT: 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.

SUBMITTER: Arold ST 

PROVIDER: S-EPMC2936596 | biostudies-literature | 2010 Sep

REPOSITORIES: biostudies-literature

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H-NS forms a superhelical protein scaffold for DNA condensation.

Arold Stefan T ST   Leonard Paul G PG   Parkinson Gary N GN   Ladbury John E JE  

Proceedings of the National Academy of Sciences of the United States of America 20100823 36


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-associat  ...[more]

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