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...
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| Published in | Proceedings of the National Academy of Sciences - PNAS Vol. 107; no. 36; pp. 15728 - 15732 |
|---|---|
| Main Authors | , , , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
National Academy of Sciences
07.09.2010
National Acad Sciences |
| Subjects | |
| Online Access | Get full text |
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| 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. |
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| AbstractList | 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. 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. [PUBLICATION ABSTRACT] |
| Author | Leonard, Paul G. Matthews, Brian W. Arold, Stefan T. Parkinson, Gary N. Ladbury, John E. |
| Author_xml | – sequence: 1 givenname: Stefan T. surname: Arold fullname: Arold, Stefan T. – sequence: 2 givenname: Paul G. surname: Leonard fullname: Leonard, Paul G. – sequence: 3 givenname: Gary N. surname: Parkinson fullname: Parkinson, Gary N. – sequence: 4 givenname: John E. surname: Ladbury fullname: Ladbury, John E. – sequence: 5 givenname: Brian W. surname: Matthews fullname: Matthews, Brian W. |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/20798056$$D View this record in MEDLINE/PubMed |
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| Copyright | Copyright © 1993-2008 The National Academy of Sciences of the United States of America Copyright National Academy of Sciences Sep 7, 2010 |
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| Notes | 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. |
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| SubjectTerms | 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 |
| Title | H-NS forms a superhelical protein scaffold for DNA condensation |
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