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.

DOI: 10.1038/nsmb989
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@article{Bradley2005StructuralBF, title={Structural basis for DNA bridging by barrier-to-autointegration factor}, author={Christina Marchetti Bradley and Donald R Ronning and Rodolfo Ghirlando and Robert Craigie and Fred Dyda}, journal={Nature Structural &Molecular Biology}, year={2005}, volume={12}, pages={935-936} }