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 oligome...

Full description

Saved in:
Bibliographic Details
Published inProceedings of the National Academy of Sciences - PNAS Vol. 107; no. 36; pp. 15728 - 15732
Main Authors Arold, Stefan T., Leonard, Paul G., Parkinson, Gary N., Ladbury, John E., Matthews, Brian W.
Format Journal Article
LanguageEnglish
Published United States National Academy of Sciences 07.09.2010
National Acad Sciences
Subjects
Acidity
Amino Acid Sequence
Bacterial Proteins - chemistry
Biochemistry
Biological Sciences
Biopolymers - chemistry
Condensation
Crystal structure
Crystallography
Crystals
Data processing
Deoxyribonucleic acid
Dimerization
Dimers
DNA
DNA - chemistry
DNA-Binding Proteins - chemistry
double prime H-NS protein
Escherichia coli
Gene expression
Models, Molecular
Molecular Sequence Data
Nucleoids
Nucleoproteins
Oligomerization
Oligomers
osmolarity
pH effects
Proteins
Scaffolds
Self-association
Sequence Homology, Amino Acid
Superhelical DNA
Temperature
Temperature effects
Transcription
Online AccessGet full text

Cover

More Information
Summary: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.
Bibliography:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ObjectType-Article-2
ObjectType-Feature-1
Edited by Brian W. Matthews, University of Oregon, Eugene, OR, and approved July 22, 2010 (received for review May 19, 2010)
2Present address: Center of Advanced Biotechnology and Medicine, University of Medicine and Dentistry of New Jersey, 679 Hoes Lane, Piscataway, New Jersey 08854
Author contributions: J.E.L. designed research; S.T.A., P.G.L., and G.N.P. performed research; S.T.A., P.G.L., and G.N.P. analyzed data; and S.T.A. and J.E.L. wrote the paper.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.1006966107