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	Mol. Cell May (2006); 22(3):363-74
The structure of the yFACT Pob3-M domain, its interaction with the DNA replication factor RPA, and a potential role in nucleosome deposition-
VanDemark AP, Blanksma M, Ferris E, Heroux A, Hill CP, Formosa T
Department of Biochemistry, University of Utah School of Medicine, Salt Lake City, 84132, USA-
Abstract: We report the crystal structure of the middle domain of the Pob3 subunit -Pob3-M- of S- cerevisiae FACT -yFACT, facilitates chromatin transcription-, which unexpectedly adopts an unusual double pleckstrin homology -PH- architecture- A mutation within a conserved surface cluster in this domain causes a defect in DNA replication that is suppressed by mutation of replication protein A -RPA-- The nucleosome reorganizer yFACT therefore interacts in a physiologically important way with the central single-strand DNA -ssDNA- binding factor RPA to promote a step in DNA replication- Purified yFACT and RPA display a weak direct physical interaction, although the genetic suppression is not explained by simple changes in affinity between the purified proteins- Further genetic analysis suggests that coordinated function by yFACT and RPA is important during nucleosome deposition- These results support the model that the FACT family has an essential role in constructing nucleosomes during DNA replication, and suggest that RPA contributes to this process-
[PUBMED: 16678108]