Structure and enzymatic properties of a stable complex of the human REV1 and REV7 proteins.

With yeast Saccharomyces cerevisiae, results from a variety of genetic and biochemical investigations have demonstrated that the REV genes play a major role in induction of mutations through replication processes that directly copy the damaged DNA template during DNA replication. However, in higher eucaryotes functions of homologues are poorly understood and appear somewhat different from the yeast case. It has been suggested that human REV1 interacts with human REV7, this being specific to higher eucaryotes. Here we show that purified human REV1 and REV7 proteins form a heterodimer in solution, which is stable through intensive purification steps. Results from biochemical analysis of the transferase reactions of the REV1-REV7 complex demonstrated, in contrast to the case of yeast Rev3 whose polymerase activity is stimulated by assembly with yeast Rev7, that human REV7 did not influence the stability, substrate specificity, or kinetic parameters of the transferase reactions of REV1 protein. The possible role of human REV7 is discussed.