Open AccessH-NS mediated compaction of DNA visualised by atomic force microscopy
Author(s) -
Remus T. Dame,
Claire Wyman,
Nora Goosen
Publication year - 2000
Publication title -
nucleic acids research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 9.008
H-Index - 537
eISSN - 1362-4954
pISSN - 0305-1048
DOI - 10.1093/nar/28.18.3504
Subject(s) - dna , nucleoid , biology , atomic force microscopy , plasmid , dna condensation , biophysics , condensation , escherichia coli , molecule , gene , crystallography , microbiology and biotechnology , nanotechnology , genetics , materials science , chemistry , transfection , physics , organic chemistry , thermodynamics
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.