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Nucleic Acids Research, 2000, Vol. 28, No. 18 3504-3510
© 2000 Oxford University Press

H-NS mediated compaction of DNA visualised by atomic force microscopy

Remus Thei Dame, Claire Wyman1 and Nora Goosen*

Laboratory of Molecular Genetics, Gorlaeus Laboratories, Leiden Institute of Chemistry, Leiden University, PO Box 9502, 2300 RA Leiden, The Netherlands and 1Department of Cell Biology and Genetics, Erasmus University, 3000 DR Rotterdam, The Netherlands

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.

* To whom correspondence should be addressed. Tel: +31 71 5274773; Fax: +31 71 5274537; Email: n.goosen@chem.leidenuniv.nl


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