Structural basis for DNA bridging by barrier-to-autointegration factor

Christina Marchetti Bradley, Donald R. Ronning, Rodolfo Ghirlando, Robert Craigie, Fred Dyda

Research output: Contribution to journalArticlepeer-review

72 Scopus citations

Abstract

The ability of barrier-to-autointegration factor (BAF) to bind and bridge DNA in a sequence-independent manner is crucial for its role in retroviral integration and a variety of cellular processes. To better understand this behavior, we solved the crystal structure of BAF bound to DNA. The structure reveals that BAF bridges DNA using two pairs of helix-hairpin-helix motifs located on opposite surfaces of the BAF dimer without changing its conformation.

Original languageEnglish (US)
Pages (from-to)935-936
Number of pages2
JournalNature Structural and Molecular Biology
Volume12
Issue number10
DOIs
StatePublished - Oct 2005
Externally publishedYes

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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