title: Recruitment to stalled replication forks of the PriA DNA helicase and replisome-loading activities is essential for survival.
abstract: PriA, a 3'-->5' superfamily 2 DNA helicase, acts to remodel stalled replication forks and as a specificity factor for origin-independent assembly of a new replisome at the stalled fork. The ability of PriA to initiate replication at stalled forked structures ensures complete genome replication and helps to protect the cell from illegitimate recombination events. This review focuses on the activities of PriA and its role in replication fork assembly and maintaining genomic integrity.
authors.affiliation: Molecular Biology Program, Weill-Cornell Graduate School of Medical Sciences, New York, NY, USA. cbg2002@med.cornell.edu
authors.forename: Carolina B
authors.initials: CB
authors.lastname: Gabbai
authors.forename: Kenneth J
authors.initials: KJ
authors.lastname: Marians
mesh_terms: D010583:Bacteriophage mu / Q000378:metabolism; D004247:DNA / Q000378:metabolism*; D004265:DNA Helicases / Q000378:metabolism*; D004261:DNA Replication; D004259:DNA-Directed DNA Polymerase / Q000378:metabolism*; D042822:Genomic Instability; D006801:Humans; D009097:Multienzyme Complexes / Q000378:metabolism*; D000099272:Replisomes
chemical_list: D004247:DNA; D004265:DNA Helicases; D004259:DNA-Directed DNA Polymerase; D009097:Multienzyme Complexes; D000099272:Replisomes