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J Biol Chem, Vol. 274, Issue 22, 15556-15561, May 28, 1999
From the Department of Biology, Universität
Konstanz, D-78457 Konstanz, Germany
Replication protein A (RPA), the major eukaryotic
single-strand specific DNA binding protein, consists of three subunits, RPA70, RPA32, and RPA14. The middle subunit, RPA32, is phosphorylated in a cell cycle-dependent manner. RPA occurs in two nuclear
compartments, bound to chromatin or free in the nucleosol. We show here
that the chromatin-associated fraction of RPA contains the
phosphorylated forms of RPA32. Treatment of chromatin with 0.4 M NaCl releases bound RPA and causes a separation of
the large and the phosphorylated middle RPA subunit. Unmodified RPA in
the nucleosolic fraction remains perfectly stable under identical
conditions. Phosphorylation is most likely an important determinant of
RPA desintegration because dialysis from 0.4 to 0.1 NaCl causes the
reformation of trimeric RPA only under dephosphorylating conditions.
Biochemical studies with isolated Cyclin-dependent protein
kinases showed that cyclin A/CDK1 and cyclin B/CDK1, but not cyclin
E/CDK2, can phosphorylate human recombinant RPA in vitro.
However, only a small fraction of in vitro phosphorylated
RPA desintegrated, suggesting that phosphorylation may be one, but
probably not the only, determinant affecting subunit interaction. We
speculate that phosphorylation and changes in subunit interaction are
required for the proposed role of RPA during the polymerase switch at
replication forks.
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