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Papers In Press, published online ahead of print January 22, 2001
Department of Developmental Biology and Oncology, Research Institute for Radiation Biology and Medicine, Hiroshima 734-8553
Corresponding Author: kkamiya{at}hiroshima-u.ac.jp
The Rev1 protein is a member of the growing family of translesion DNA polymerases. A cDNA of the human REV1 gene that we had originally isolated encoded 1250 amino acids residues, which was one amino acid shorter than previously reported ones. The shorter form of Rev1 was named Rev1S. All individuals examined expressed equivalent amounts of REV1S and REV1 mRNA, suggesting that the REV1S mRNA is a splicing variant. We show that the Rev1S protein also possesses deoxycytidyl transferase activity that inserts a dCMP opposite a DNA template apurinic/apyrimidinic (AP) site. Deletion and point mutation analysis of the Rev1S protein revealed that the domain required for deoxycytidyl transferase and DNA binding activities of the Rev1S protein are located in a conserved domain of translesion DNA polymerases. This result indicates that the structure of the catalytic site of the deoxycytidyl transferase closely resembles that of the translesion DNA polymerases. Therefore, the molecular mechanism of the dCMP transfer reaction of the Rev1S protein, and maybe also the Rev1 protein, might be the same as that of the dNTP transfer reaction of the translesion DNA polymerases.
J. Biol. Chem, 10.1074/jbc.M008082200
Submitted on September 5, 2000
Revised on December 7, 2000
Accepted on January 19, 2001
Deoxycytidyl transferase activity of the human Rev1 protein is closely associated with the conserved polymerase domain
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