H-NS forms a superhelical protein scaffold for DNA condensation.
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.
Arold
Stefan T
ST
Department of Biochemistry and Molecular Biology, University of Texas, M. D. Anderson Cancer Center, Houston, 77030, USA.
Leonard
Paul G
PG
Parkinson
Gary N
GN
Ladbury
John E
JE
D000595:Amino Acid Sequence; D001426:Bacterial Proteins / Q000737:chemistry*; D001704:Biopolymers / Q000737:chemistry; D004247:DNA / Q000737:chemistry*; D004268:DNA-Binding Proteins / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017386:Sequence Homology, Amino Acid; D013696:Temperature
D001426:Bacterial Proteins; D001704:Biopolymers; D004268:DNA-Binding Proteins; C031908:H-NS protein, bacteria; D004247:DNA
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