期刊
GENES TO CELLS
卷 17, 期 9, 页码 790-806出版社
WILEY-BLACKWELL
DOI: 10.1111/j.1365-2443.2012.01628.x
关键词
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DNA polymerase mu (pol mu) catalyzes nonhomologous end-joining in DNA double-stranded break repair. Pol mu consists of an amino-terminal BRCA1 carboxyl-terminal homology (BRCT) domain and a pol beta-like region, which contains the catalytic site. By DNA cellulose column chromatography, using full-length pol mu and five different deletion mutants, we found that the amino-terminal region has double-stranded DNA (dsDNA)-binding activity. Pol mu without BRCT domain reduces the DNA polymerization activity when compared to full-length pol mu. Observation by atomic force microscopy showed that full-length pol mu binds to the ends and middle part of dsDNA. Pol mu 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 dsDNA (mpdDNA). Terminal deoxynucleotidyltransferase, which, like pol mu, belongs to the X family DNA polymerases, also bound to mpdDNA through its amino-terminal region.
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