Three residues of the interdomain linker determine the conformation and single-base deletion fidelity of Y-family translesion polymerases.

ABSTRACT: Dpo4 and Dbh are from two closely related Sulfolobus species and are well studied archaeal homologues of pol IV, an error prone Y-family polymerase from Escherichia coli. Despite sharing 54% amino acid identity, these polymerases display distinct mutagenic and translesion specificities. Structurally, Dpo4 and Dbh adopt different conformations because of the difference in relative orientation of their N-terminal catalytic and C-terminal DNA binding domains. Using chimeric constructs of these two polymerases, we have previously demonstrated that the interdomain linker is a major determinant of polymerase conformation, base-substitution fidelity, and abasic-site translesion synthesis. Here we find that the interdomain linker also affects the single-base deletion frequency and the mispair exte

SUBMITTER: Mukherjee P 

PROVIDER: S-EPMC3945299 | biostudies-literature | 2014 Mar

REPOSITORIES: biostudies-literature