Uracil recognition by archaeal family B DNA polymerases.
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.
Connolly
B A
BA
School of Cell and Molecular Biosciences, University of Newcastle, Newcastle upon Tyne NE2 4HH, UK. b.a.connolly@ncl.ac.uk
Fogg
M J
MJ
Shuttleworth
G
G
Wilson
B T
BT
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*
D014498:Uracil; D004259:DNA-Directed DNA Polymerase; D011755:Pyrophosphatases; C020020:dUTP pyrophosphatase