title: Role of single-stranded DNA in targeting REV1 to primer termini.
abstract: Cellular functions of the REV1 gene have been conserved in evolution and appear important for maintaining genetic integrity through translesion DNA synthesis. This study documents a novel biochemical activity of human REV1 protein, due to higher affinity for single-stranded DNA (ssDNA) than the primer terminus. Preferential binding to long ssDNA regions of the template strand means that REV1 is targeted specifically to the included primer termini, a property not shared by other DNA polymerases, including human DNA polymerases alpha, beta, and eta. Furthermore, a mutant REV1 lacking N- and C-terminal domains, but catalytically active, lost this function, indicating that control is not due to the catalytic core. The novel activity of REV1 protein might imply a role for ssDNA in the regulation of translesion DNA synthesis.
authors.affiliation: Research Institute for Radiation Biology and Medicine, Hiroshima University, Hiroshima 734-8553, Japan.
authors.forename: Yuji
authors.initials: Y
authors.lastname: Masuda
authors.forename: Kenji
authors.initials: K
authors.lastname: Kamiya
mesh_terms: D001665:Binding Sites; D002384:Catalysis; D004261:DNA Replication; D004277:DNA, Single-Stranded / Q000235:genetics / Q000378:metabolism*; D004926:Escherichia coli; D006801:Humans; D009154:Mutation; D009687:Nuclear Proteins; D009713:Nucleotidyltransferases / Q000235:genetics / Q000378:metabolism*; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D013379:Substrate Specificity; D000099270:Y-Family DNA Polymerases
chemical_list: D004277:DNA, Single-Stranded; D009687:Nuclear Proteins; D009713:Nucleotidyltransferases; C429004:REV1 protein, human; D000099270:Y-Family DNA Polymerases