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- W2022726084 abstract "DNA polymerase μ (pol μ) catalyzes nonhomologous end‐joining in DNA double‐stranded break repair. Pol μ consists of an amino‐terminal BRCA 1 carboxyl‐terminal homology ( BRCT ) domain and a pol β‐like region, which contains the catalytic site. By DNA cellulose column chromatography, using full‐length pol μ and five different deletion mutants, we found that the amino‐terminal region has double‐stranded DNA (ds DNA )‐binding activity. Pol μ without BRCT domain reduces the DNA polymerization activity when compared to full‐length pol μ. Observation by atomic force microscopy showed that full‐length pol μ binds to the ends and middle part of ds DNA . Pol μ lacking the amino‐terminal region or with a mutation within the BRCT domain bound only to DNA ends, whereas the amino‐terminal region with the BRCT domain bound to both the ends and the middle part of ds DNA (mpd DNA ). Terminal deoxynucleotidyltransferase, which, like pol μ, belongs to the X family DNA polymerases, also bound to mpd DNA through its amino‐terminal region." @default.
- W2022726084 created "2016-06-24" @default.
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- W2022726084 date "2012-08-16" @default.
- W2022726084 modified "2023-10-04" @default.
- W2022726084 title "<scp>BRCT</scp> domain of <scp>DNA</scp> polymerase μ has <scp>DNA</scp>‐binding activity and promotes the <scp>DNA</scp> polymerization activity" @default.
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- W2022726084 doi "https://doi.org/10.1111/j.1365-2443.2012.01628.x" @default.
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