title: Uracil recognition by archaeal family B DNA polymerases.
abstract: Archaeal family-B DNA polymerases possess a novel uracil-sensing mechanism. A specialized pocket scans the template, ahead of the replication fork, for the presence of uracil; on encountering this base, DNA synthesis is stalled. The structural basis for uracil recognition by polymerases is described and compared with other uracil-recognizing enzymes (uridine-triphosphate pyrophophatases and uracil-DNA glycosylases). Remarkably, protein-protein interactions between all three archaeal uracil sensors are observed; possibly the enzymes co-operate to efficiently eliminate uracil from archaeal genomes.
authors.affiliation: School of Cell and Molecular Biosciences, University of Newcastle, Newcastle upon Tyne NE2 4HH, UK. b.a.connolly@ncl.ac.uk
authors.forename: B A
authors.initials: BA
authors.lastname: Connolly
authors.forename: M J
authors.initials: MJ
authors.lastname: Fogg
authors.forename: G
authors.initials: G
authors.lastname: Shuttleworth
authors.forename: B T
authors.initials: BT
authors.lastname: Wilson
mesh_terms: D001105:Archaea / Q000201:enzymology*; D004260:DNA Repair / Q000235:genetics; D004259:DNA-Directed DNA Polymerase / Q000737:chemistry* / Q000378:metabolism*; D008958:Models, Molecular; D011487:Protein Conformation; D011755:Pyrophosphatases / Q000737:chemistry / Q000378:metabolism; D013379:Substrate Specificity; D014498:Uracil / Q000378:metabolism*
chemical_list: D014498:Uracil; D004259:DNA-Directed DNA Polymerase; D011755:Pyrophosphatases; C020020:dUTP pyrophosphatase