Molecular events during translocation and proofreading extracted from 200 static structures of DNA polymerase.
DNA polymerases in family B are workhorses of DNA replication that carry out the bulk of the job at a high speed with high accuracy. A polymerase in this family relies on a built-in exonuclease for proofreading. It has not been observed at the atomic resolution how the polymerase advances one nucleotide space on the DNA template strand after a correct nucleotide is incorporated, that is, a process known as translocation. It is even more puzzling how translocation is avoided after the primer strand is excised by the exonuclease and returned back to the polymerase active site once an error occurs. The structural events along the bifurcate pathways of translocation and proofreading have been unwittingly captured by hundreds of structures in Protein Data Bank. This study analyzes all available structures of a representative member in family B and reveals the orchestrated event sequence during translocation and proofreading.
Department of Chemistry, The University of Illinois at Chicago, Chicago, IL 60607, USA Renz Research, Inc., Westmont, IL 60559, USA zren@uic.edu.
Zhong
Z
Ren
D020134:Catalytic Domain; D004247:DNA / Q000096:biosynthesis / Q000737:chemistry / Q000378:metabolism; D004259:DNA-Directed DNA Polymerase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D030562:Databases, Protein; D008958:Models, Molecular; D009154:Mutation; D013698:Templates, Genetic
D004247:DNA; D004259:DNA-Directed DNA Polymerase