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

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.

DOI: 10.1073/pnas.1006966107

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.

Item Type:Article
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
ID Code:2975
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

Statistics

Item downloaded times since 16 Mar 2012 08:53.

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


Repository Staff Only: Item control page

School of Pharmacy Staff Only: Edit a copy to replace this item