Publications

• Deoxycytidyl transferase activity of yeast REV1 protein.

  Nelson J.R., Lawrence C.W., Hinkle D.C.

  Mutagenesis induced by DNA damage in Saccharomyces cerevisiae requires the products of the REV1, REV3 and REV7 genes. The Rev3 and Rev7 proteins are subunits of DNA polymerase-zeta (Pol-zeta), an enzyme whose sole function appears to be translesion synthesis. Rev1 protein has weak homology with Um ... >> More

  Mutagenesis induced by DNA damage in Saccharomyces cerevisiae requires the products of the REV1, REV3 and REV7 genes. The Rev3 and Rev7 proteins are subunits of DNA polymerase-zeta (Pol-zeta), an enzyme whose sole function appears to be translesion synthesis. Rev1 protein has weak homology with UmuC protein which facilitates translesion synthesis in Escherichia coli by an unknown mechanism. We show here that Rev1 protein has a deoxycytidyl transferase activity which transfers a dCMP residue from dCTP to the 3' end of a DNA primer in a template-dependent reaction. Efficient transfer occurred opposite a template abasic site, but approximately 20% transfer also occurred opposite a template guanine and approximately 10% opposite adenine or uracil; < or = 1% was seen opposite thymine or cytosine. Insertion of cytosine opposite an abasic site produced a terminus that was extended efficiently by Pol-zeta, but not by yeast Pol-alpha. << Less

  Nature 382:729-731(1996) [PubMed] [EuropePMC]

• The human REV1 gene codes for a DNA template-dependent dCMP transferase.

  Lin W., Xin H., Zhang X., Wu X., Yuan F., Wang Z.

  DNA is frequently damaged by various physical and chemical agents. DNA damage can lead to mutations during replication. In the yeast Saccharomyces cerevisiae, the damage-induced mutagenesis pathway requires the Rev1 protein. We have isolated a human cDNA homologous to the yeast REV1 gene. The huma ... >> More

  DNA is frequently damaged by various physical and chemical agents. DNA damage can lead to mutations during replication. In the yeast Saccharomyces cerevisiae, the damage-induced mutagenesis pathway requires the Rev1 protein. We have isolated a human cDNA homologous to the yeast REV1 gene. The human REV1 cDNA consists of 4255 bp and codes for a protein of 1251 amino acid residues with a calculated molecular weight of 138 248 Da. The human REV1 gene is localized between 2q11.1 and 2q11.2. We show that the human REV1 protein is a dCMP transferase that specifically inserts a dCMP residue opposite a DNA template G. In addition, the human REV1 transferase is able to efficiently and specifically insert a dCMP opposite a DNA template apurinic/apyrimidinic (AP) site or a uracil residue. These results suggest that the REV1 transferase may play a critical role during mutagenic translesion DNA synthesis bypassing a template AP site in human cells. Consistent with its role as a fundamental mutagenic protein, the REV1 gene is ubiquitously expressed in various human tissues. << Less

  Nucleic Acids Res. 27:4468-4475(1999) [PubMed] [EuropePMC]

• Mechanisms of dCMP transferase reactions catalyzed by mouse Rev1 protein.

  Masuda Y., Takahashi M., Fukuda S., Sumii M., Kamiya K.

  The Rev1 protein, a member of a large family of translesion DNA polymerases, catalyzes a dCMP transfer reaction. Recombinant mouse Rev1 protein was found to insert a dCMP residue opposite guanine, adenine, thymine, cytosine, uracil, and an apurinic/apyrimidinic site and to have weak ability for tr ... >> More

  The Rev1 protein, a member of a large family of translesion DNA polymerases, catalyzes a dCMP transfer reaction. Recombinant mouse Rev1 protein was found to insert a dCMP residue opposite guanine, adenine, thymine, cytosine, uracil, and an apurinic/apyrimidinic site and to have weak ability for transfer to a mismatched terminus. The mismatch-extension ability was strongly enhanced by a guanine residue on the template near the mismatched terminus; this was not the case with an apurinic/apyrimidinic site and the other template nucleotides. Kinetic analysis of the dCMP transferase reaction provided evidence for high affinity for dCTP with template G but not the other templates, whereas the template nucleotide did not much affect the V(max) value. Furthermore, it could be established that the mouse Rev1 protein inserts dGMP and dTMP residues opposite template guanine at a V(max) similar to that for dCMP. << Less

  J. Biol. Chem. 277:3040-3046(2002) [PubMed] [EuropePMC]