Arold, S.T., Leonard, P.G., Parkinson, G.N. and Ladbury, J.E. (2010) H-NS forms a superhelical protein scaffold for DNA condensation. Proceedings of the National Academy of Sciences of the United States of America, 107 (36). pp. 15728-15732. 10.1073/pnas.1006966107.
Full text not available from this repository.
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.
|Uncontrolled Keywords:||chromatin DNA binding nucleoid supercoil transcriptional regulation|
|Departments, units and centres:||Department of Pharmaceutical and Biological Chemistry > Department of Pharmaceutical and Biological Chemistry|
|Journal or Publication Title:||Proceedings of the National Academy of Sciences of the United States of America|
|Deposited By:||Library Staff|
|Deposited On:||16 Mar 2012 08:53|
|Last Modified:||16 Mar 2012 08:53|
Item downloaded times since 16 Mar 2012 08:53.
Repository Staff Only: Item control page
School of Pharmacy Staff Only: Edit a copy to replace this item