Nucleic Acids Research, Vol 27, Issue 24 4695-4702, Copyright © 1999 by Oxford University Press
I Hayashi, K Morikawa and Y Ishino
Pyrococcus furiosus has an operon containing the DNA polymerase II (PolD)
gene and three other genes. Using a two-hybrid screening to examine the
interactions of the proteins encoded by the operon, we identified a
specific interaction between the second subunit of PolD (DP1) and a
Rad51/Dmc1 homologous protein (RadB). To ensure the specific interaction
between these two proteins, each gene in the operon was expressed in
Escherichia coli or insect cells separately and the products were purified.
The in vitro analyses using the purified proteins also showed the
interaction between DP1 and RadB. The deletion mutant analysis of DP1
revealed that a region important for binding with RadB is located in the
central part of the sequence (amino acid residues 206-498). This region has
an overlap to the C-terminal half (amino acids 334-613), which is highly
conserved among euryarchaeal DP1s and is essential for the activity of
PolD. Our results suggest that, although RadB does not noticeably affect
the primer extension ability of PolD in vitro, PolD may utilize the RadB
protein in DNA synthesis under certain conditions.
ARTICLES
Specific interaction between DNA polymerase II (PolD) and RadB, a Rad51/Dmc1 homolog, in Pyrococcus furiosus
Department of Molecular Biology, Biomolecular Engineering Research Institute (BERI), 6-2-3, Furuedai, Suita, Osaka 565-0874, Japan.
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