PMID:10982869
| Citation |
Dame, RT, Wyman, C and Goosen, N (2000) H-NS mediated compaction of DNA visualised by atomic force microscopy. Nucleic Acids Res. 28:3504-10 |
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| Abstract |
The Escherichia coli H-NS protein is a nucleoid-associated protein involved in gene regulation and DNA compaction. To get more insight into the mechanism of DNA compaction we applied atomic force microscopy (AFM) to study the structure of H-NS-DNA complexes. On circular DNA molecules two different levels of H-NS induced condensation were observed. H-NS induced lateral condensation of large regions of the plasmid. In addition, large globular structures were identified that incorporated a considerable amount of DNA. The formation of these globular structures appeared not to be dependent on any specific sequence. On the basis of the AFM images, a model for global condensation of the chromosomal DNA by H-NS is proposed. |
| Links | |
| Keywords |
Bacterial Proteins/metabolism; Bacterial Proteins/physiology; Bacterial Proteins/ultrastructure; DNA/chemistry; DNA/metabolism; DNA/ultrastructure; DNA-Binding Proteins/metabolism; DNA-Binding Proteins/physiology; DNA-Binding Proteins/ultrastructure; Escherichia coli; Microscopy, Atomic Force; Nucleic Acid Conformation; Protein Binding; Protein Conformation |
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