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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.

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Figure 1: Crystal structure of BAF–7-mer dsDNA complex.
Figure 2: Model for DNA condensation by BAF.

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Acknowledgements

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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Correspondence to Fred Dyda.

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Supplementary information

Supplementary Fig. 1

Size exclusion chromatography of the BAF-7 bp DNA complex (PDF 98 kb)

Supplementary Fig. 2

Sedimentation equilibrium data for BAF-DNA complexes (PDF 284 kb)

Supplementary Fig. 3

Size exclusion chromatography of the BAF-9 bp DNA complex (PDF 44 kb)

Supplementary Fig. 4

Electron density map of the BAF-7 bp DNA complex (PDF 55 kb)

Supplementary Table 1

Sedimentation equilibrium data for BAF-DNA complexes (PDF 24 kb)

Supplementary Table 2

Crystallographic data collection and statistics (PDF 15 kb)

Supplementary Methods (PDF 38 kb)

Supplementary Discussion

Solution characterization of BAF-DNA complexes (PDF 22 kb)

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Bradley, C., Ronning, D., Ghirlando, R. et al. Structural basis for DNA bridging by barrier-to-autointegration factor. Nat Struct Mol Biol 12, 935–936 (2005). https://doi.org/10.1038/nsmb989

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