H-NS forms a superhelical protein scaffold for DNA condensation

• Published in: Proceedings 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
• Language: English
• 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

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...