title: Recognition of deaminated bases by archaeal family-B DNA polymerases.
abstract: Archaeal family-B DNA polymerases interact specifically with uracil and hypoxanthine, stalling replication on encountering these deaminated bases in DNA template strands. The present review describes X-ray structural data which elucidate the mechanism of read-ahead recognition of uracil and suggests how this is coupled to cessation of polymerization. The possible role of read-ahead recognition of uracil/hypoxanthine in DNA repair is discussed, as is the observation that the feature appears to be limited to replicative polymerases of the archaeal domain.
authors.affiliation: Institute for Cell and Molecular Biosciences (ICaMB), University of Newcastle, Newcastle upon Tyne NE2 4HH, UK. b.a.connolly@ncl.ac.uk
authors.forename: Bernard A
authors.initials: BA
authors.lastname: Connolly
mesh_terms: D001105:Archaea / Q000201:enzymology*; D019843:Archaeal Proteins / Q000737:chemistry / Q000378:metabolism*; D004259:DNA-Directed DNA Polymerase / Q000737:chemistry / Q000378:metabolism*; D003641:Deamination; D011687:Purines / Q000378:metabolism*; D011743:Pyrimidines / Q000378:metabolism*
chemical_list: D019843:Archaeal Proteins; D011687:Purines; D011743:Pyrimidines; D004259:DNA-Directed DNA Polymerase