Low-force DNA condensation and discontinuous high-force decondensation reveal a loop-stabilizing function of the protein fis

Dunja Skoko*, Jie Yan, Reid C. Johnson, John F. Marko

*Corresponding author for this work

Research output: Contribution to journalArticle

49 Scopus citations

Abstract

We report single-DNA-stretching experiments showing that the protein Fis, an abundant bacterial chromosome protein of E. coli, mediates a dramatic DNA condensation to zero length. This condensation occurs abruptly when DNA tension is reduced below a protein-concentration-dependent threshold f*<1pN. Following condensation, reopening under larger forces proceeds via a series of discrete jumps, indicating that Fis is able to stabilize DNA crossings. Our experiments suggest that Fis may play a role in vivo stabilizing the "loop-domain" structure of the bacterial chromosome.

Original languageEnglish (US)
Article number208101
JournalPhysical review letters
Volume95
Issue number20
DOIs
StatePublished - Nov 11 2005

ASJC Scopus subject areas

  • Physics and Astronomy(all)

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