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Originally published In Press as doi:10.1074/jbc.M112146200 on February 15, 2002

J. Biol. Chem., Vol. 277, Issue 18, 15546-15551, May 3, 2002
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Yeast Rev1 Protein Is a G Template-specific DNA Polymerase*

Lajos Haracska, Satya Prakash, and Louise PrakashDagger

From the Sealy Center for Molecular Science, University of Texas Medical Branch, Galveston, Texas 77555-1061

Rev1 protein of Saccharomyces cerevisiae functions with DNA polymerase zeta  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 ~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.

* This work was supported by National Institutes of Health Grant GM19261.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed: Sealy Center for Molecular Science, University of Texas Medical Branch, 6.104 Medical Research Bldg., 11th and Mechanic St., Galveston, TX 77555-1061. Tel.: 409-747-8601; Fax: 409-747-8608; E-mail: lprakash@scms.utmb.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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