期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 277, 期 18, 页码 15546-15551出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M112146200
关键词
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资金
- NIGMS NIH HHS [GM19261] Funding Source: Medline
Rev1 protein of Saccharomyces cerevisiae functions with DNA polymerase in mutagenic trans-lesion synthesis. Because of the reported preferential incorporation of a C residue opposite an abasic site, Rev1 has been referred to as a deoxycytidyltransferase. Here, we use steady-state kinetics to examine nucleotide incorporation by Rev1 opposite undamaged and damaged template residues. We show that Rev1 specifically inserts a C residue opposite template G, and it is similar to25-, 40-, and 400-fold less efficient at inserting a C residue opposite an abasic site, an O-6-methylguanine, and an 8-oxoguanine lesion, respectively. Rev1 misincorporates G, A, and T residues opposite template G with a frequency of similar to10(-3) to 10(-4). Consistent with this finding, Rev1 replicates DNA containing a string of Gs in a template-specific manner, but it has a low processivity incorporating 1.6 nucleotides per DNA binding event on the average. From these observations, we infer that Rev1 is a G template-specific DNA polymerase.
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