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Structure and Function of Y Family DNa Polymerases
Author(s) -
Walker Graham Charles,
Jarosz Daniel,
Simon Sharotka,
Waters Lauren,
D'Souza Sanjay,
Wiltrout Mary Ellen
Publication year - 2007
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.21.5.a91-b
Subject(s) - dna polymerase , mutagenesis , biology , genetics , dna replication , dna polymerase ii , polymerase , dna synthesis , dna , dna polymerase mu , dna clamp , mutation , microbiology and biotechnology , reverse transcriptase , gene , polymerase chain reaction , circular bacterial chromosome
Our observation that dinB mutants are sensitive to nitrofurazone led us to the discovery that E. coli DinB (DNA pol IV), as well as the mammalian ortholog DNA pol kappa, are much better polymerases opposite N 2 ‐ furfuryl‐dG than opposite ordinary dG. Our additional discovery that a single mutation can eliminate DinB's ability to carry our this type of translesion synthesis without affecting its ability to copy ordinary DNA suggests that the biological role of the DinB family is to carry out relatively accurate DNA synthesis over a common class of N 2 ‐dG adducts common to all three domains of life. The Saccharomyces cerevisiae Rev1 protein is a Family Y DNA polymerase that lies at the root of mutagenesis in eukaryotes, carrying out limited translesion synthesis itself, but more importantly, serving as a scaffold to recruit other translesion DNA polymerases. We have discovered that Rev1 levels vary striking during the cell cycle, being very low in G1, and then peaking at 50‐fold higher levels during G2/M.