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

Nucleic Acids Res. 2000 Sep 15;28(18):3504-10. doi: 10.1093/nar/28.18.3504.

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.

MeSH terms

  • 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

Substances

  • Bacterial Proteins
  • DNA-Binding Proteins
  • H-NS protein, bacteria
  • DNA