A divalent switch drives H-NS/DNA-binding conformations between stiffening and bridging modes

Yingjie Liu, Hu Chen, Linda Kenney, Jie Yan

Research output: Contribution to journalArticle

141 Citations (Scopus)

Abstract

Heat-stable nucleoid structuring protein (H-NS) is an abundant prokaryotic protein that plays important roles in organizing chromosomal DNA and gene silencing. Two controversial binding modes were identified. H-NS binding stimulating DNA bridging has become the accepted mechanism, whereas H-NS binding causing DNA stiffening has been largely ignored. Here, we report that both modes exist, and that changes in divalent cations drive a switch between them. The stiffening formis present under physiological conditions, and directly responds to pH and temperature in vitro. Our findings have broad implications and require a reinterpretation of the mechanism by which H-NS regulates genes.

Original languageEnglish (US)
Pages (from-to)339-344
Number of pages6
JournalGenes and Development
Volume24
Issue number4
DOIs
StatePublished - Feb 15 2010
Externally publishedYes

Fingerprint

Nucleic Acid Conformation
Hot Temperature
DNA-Binding Proteins
Proteins
Divalent Cations
Gene Silencing
Temperature
DNA

Keywords

  • Atomic force
  • Gene silencing
  • Heat-stable nucleoid structuring protein (H-NS)
  • Magnetic tweezers
  • Microscopy
  • Pathogenicity islands
  • Transcriptional regulation

ASJC Scopus subject areas

  • Genetics
  • Developmental Biology

Cite this

A divalent switch drives H-NS/DNA-binding conformations between stiffening and bridging modes. / Liu, Yingjie; Chen, Hu; Kenney, Linda; Yan, Jie.

In: Genes and Development, Vol. 24, No. 4, 15.02.2010, p. 339-344.

Research output: Contribution to journalArticle

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