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PDBsum entry 2gcl
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References listed in PDB file
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Key reference
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Title
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The structure of the yfact pob3-M domain, Its interaction with the DNA replication factor rpa, And a potential role in nucleosome deposition.
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Authors
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A.P.Vandemark,
M.Blanksma,
E.Ferris,
A.Heroux,
C.P.Hill,
T.Formosa.
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Ref.
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Mol Cell, 2006,
22,
363-374.
[DOI no: ]
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PubMed id
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Abstract
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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.
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Figure 5.
Figure 5. Physical Interaction between yFACT and RPA
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Figure 6.
Figure 6. Effects of Histone Overexpression or Mutation
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The above figures are
reprinted
by permission from Cell Press:
Mol Cell
(2006,
22,
363-374)
copyright 2006.
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