Role of Single-stranded DNA in Targeting REV1 to Primer Termini

• Published in: The Journal of biological chemistry Vol. 281; no. 34; pp. 24314 - 24321
• Main Authors: Masuda, Yuji, Kamiya, Kenji
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 25.08.2006; American Society for Biochemistry and Molecular Biology
• Subjects: Binding Sites; Catalysis; DNA Replication; DNA, Single-Stranded - genetics; DNA, Single-Stranded - metabolism; Escherichia coli; Humans; Mutation; Nuclear Proteins; Nucleotidyltransferases - genetics; Nucleotidyltransferases - metabolism; Protein Binding; Protein Structure, Tertiary; Substrate Specificity
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1074/jbc.M602967200

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 α, β, and η. 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.