Structural basis for DNA bridging by barrier-to-autointegration factor.
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.
Bradley
Christina Marchetti
CM
Laboratory of Molecular Biology, National Institute of Diabetes & Digestive & Kidney Diseases, US National Institutes of Health (NIH), 5 Center Drive, Bethesda, Maryland 20892, USA.
Ronning
Donald R
DR
Ghirlando
Rodolfo
R
Craigie
Robert
R
Dyda
Fred
F
D000595:Amino Acid Sequence; D003461:Crystallography; D004247:DNA / Q000737:chemistry* / Q000378:metabolism; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000378:metabolism; D018257:Helix-Loop-Helix Motifs; D006801:Humans; D008969:Molecular Sequence Data; D009687:Nuclear Proteins / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation
C501959:BANF1 protein, human; D004268:DNA-Binding Proteins; D009687:Nuclear Proteins; D004247:DNA