Open AccessRole of the Pif1-PCNA Complex in Pol δ-Dependent Strand Displacement DNA Synthesis and Break-Induced Replication
Author(s) -
Olga Buzovetsky,
Youngho Kwon,
Nhung Pham,
Claire Kim,
Grzegorz Ira,
Patrick Sung,
Yong Xiong
Publication year - 2017
Publication title -
cell reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 6.264
H-Index - 154
eISSN - 2639-1856
pISSN - 2211-1247
DOI - 10.1016/j.celrep.2017.10.079
Subject(s) - processivity , dna polymerase , proliferating cell nuclear antigen , dna polymerase delta , dna replication , replication protein a , dna clamp , biology , replication factor c , dna repair , microbiology and biotechnology , dna mismatch repair , dna , eukaryotic dna replication , genetics , dna binding protein , reverse transcriptase , polymerase chain reaction , gene , transcription factor
The S. cerevisiae Pif1 helicase functions with DNA polymerase (Pol) δ in DNA synthesis during break-induced replication (BIR), a conserved pathway responsible for replication fork repair and telomere recombination. Pif1 interacts with the DNA polymerase processivity clamp PCNA, but the functional significance of the Pif1-PCNA complex remains to be elucidated. Here, we solve the crystal structure of PCNA in complex with a non-canonical PCNA-interacting motif in Pif1. The structure guides the construction of a Pif1 mutant that is deficient in PCNA interaction. This mutation impairs the ability of Pif1 to enhance DNA strand displacement synthesis by Pol δ in vitro and also the efficiency of BIR in cells. These results provide insights into the role of the Pif1-PCNA-Pol δ ensemble during DNA break repair by homologous recombination.
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