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

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

doi:10.1038/nsmb989

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 journal › Article › peer-review

95 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 language	English (US)
Pages (from-to)	935-936
Number of pages	2
Journal	Nature Structural and Molecular Biology
Volume	12
Issue number	10
DOIs	https://doi.org/10.1038/nsmb989
State	Published - Oct 2005
Externally published	Yes

ASJC Scopus subject areas

Structural Biology
Molecular Biology

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title = "Structural basis for DNA bridging by barrier-to-autointegration factor",

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.",

author = "Bradley, {Christina Marchetti} and Ronning, {Donald R.} and Rodolfo Ghirlando and Robert Craigie and Fred Dyda",

note = "Funding Information: We thank A. Burgess Hickman, Y. Suzuki, M. Li and T. Chiu for helpful discussions. C.B. is a Paul Sigler/Argoron Fellow of the Helen Hay Whitney Foundation. This study used the helix computational systems at the Center for Information Technology, NIH, and was supported by the NIH Intramural AIDS Targeted Antiviral Program.",

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AU - Bradley, Christina Marchetti

AU - Ronning, Donald R.

AU - Ghirlando, Rodolfo

AU - Craigie, Robert

AU - Dyda, Fred

N1 - Funding Information: We thank A. Burgess Hickman, Y. Suzuki, M. Li and T. Chiu for helpful discussions. C.B. is a Paul Sigler/Argoron Fellow of the Helen Hay Whitney Foundation. This study used the helix computational systems at the Center for Information Technology, NIH, and was supported by the NIH Intramural AIDS Targeted Antiviral Program.

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N2 - 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.

AB - 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.

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

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