Yeast Rev1 protein is a G template-specific DNA polymerase

Lajos Haracska, Satya Prakash, Louise Prakash

Research output: Contribution to journalArticlepeer-review

127 Scopus citations


Rev1 protein of Saccharomyces cerevisiae functions with DNA polymerase ζ in mutagenic trans-lesion synthesis. Because of the reported preferential incorporation of a C residue opposite an a basic 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 ∼25-, 40-, and 400-fold less efficient at inserting a C residue opposite an abasic site, an O6-methylguanine, and an 8-oxoguanine lesion, respectively. Rev1 misincorporates G, A, and T residues opposite template G with a frequency of ∼10-3 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.

Original languageEnglish (US)
Pages (from-to)15546-15551
Number of pages6
JournalJournal of Biological Chemistry
Issue number18
StatePublished - May 3 2002

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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