Studies on the base excision repair (BER) complex in Pyrococcus furiosus.
We have been studying the functions of PCNA (proliferating-cell nuclear antigen) for the assembly and reassembly of the replisome during replication fork progression. We have identified the functional interactions between PCNA and several proteins involved in DNA replication and repair from Pyrococcus furiosus. We recently reported that the activity of UDG (uracil-DNA glycosylase) in P. furiosus (PfuUDG) is stimulated by PCNA (PfuPCNA) in vitro, and identified an atypical PCNA-binding site, AKTLF, in the PfuUDG protein. To understand further the function of the complex in the BER (base excision repair) process, we investigated the AP (apurinic/apyrimidinic) endonuclease, which can process the BER pathway after uracil removal by UDG. Interestingly, one candidate ORF (open reading frame) for the AP endonuclease was found in the operon containing the gene encoding UDG in the P. furiosus genome. However, this ORF did not exhibit any activity. Instead, we identified the AP endonuclease activity from the other candidate gene products, and designated the protein as PfuAP. We discovered a physical interaction between PfuAP and PfuPCNA, suggesting the formation of a BER complex in one of the repair systems in P. furiosus.
Kiyonari
Shinichi
S
Department of Genetic Resources Technology, Kyushu University, 6-10-1 Hakozaki, Fukuoka-shi, Fukuoka 812-8581, Japan.
Tahara
Saki
S
Uchimura
Maiko
M
Shirai
Tsuyoshi
T
Ishino
Sonoko
S
Ishino
Yoshizumi
Y
D004260:DNA Repair; D018809:Proliferating Cell Nuclear Antigen / Q000737:chemistry / Q000378:metabolism; D011485:Protein Binding; D020027:Pyrococcus furiosus / Q000201:enzymology / Q000378:metabolism*; D051981:Uracil-DNA Glycosidase / Q000737:chemistry / Q000378:metabolism
D018809:Proliferating Cell Nuclear Antigen; D051981:Uracil-DNA Glycosidase