title: Accessory replicative helicases and the replication of protein-bound DNA.
abstract: Complete, accurate duplication of the genetic material is a prerequisite for successful cell division. Achieving this accuracy is challenging since there are many barriers to replication forks that may cause failure to complete genome duplication or result in possibly catastrophic corruption of the genetic code. One of the most important types of replicative barriers are proteins bound to the template DNA, especially transcription complexes. Removal of these barriers demands energy input not only to separate the DNA strands but also to disrupt multiple bonds between the protein and DNA. Replicative helicases that unwind the template DNA for polymerases at the fork can displace proteins bound to the template. However, even occasional failures in protein displacement by the replicative helicase could spell disaster. In such circumstances, failure to restart replication could result in incomplete genome duplication. Avoiding incomplete genome duplication via the repair and restart of blocked replication forks also challenges viability since the involvement of recombination enzymes is associated with the risk of genome rearrangements. Organisms have therefore evolved accessory replicative helicases that aid replication fork movement along protein-bound DNA. These helicases reduce the dangers associated with replication blockage by protein-DNA complexes, aiding clearance of blocks and resumption of replication by the same replisome thus circumventing the need for replication repair and restart. This review summarises recent work in bacteria and eukaryotes that has begun to delineate features of accessory replicative helicases and their importance in genome stability.
authors.affiliation: Department of Biology, University of York, Wentworth Way, York YO10 5DD, United Kingdom.
authors.forename: Jan-Gert
authors.initials: JG
authors.lastname: Brüning
authors.affiliation: Department of Biology, University of York, Wentworth Way, York YO10 5DD, United Kingdom.
authors.forename: Jamieson L
authors.initials: JL
authors.lastname: Howard
authors.affiliation: Department of Biology, University of York, Wentworth Way, York YO10 5DD, United Kingdom. Electronic address: peter.mcglynn@york.ac.uk.
authors.forename: Peter
authors.initials: P
authors.lastname: McGlynn
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism; D004247:DNA / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D004265:DNA Helicases / Q000737:chemistry / Q000378:metabolism*; D004261:DNA Replication; D004268:DNA-Binding Proteins / Q000737:chemistry / Q000378:metabolism*; D008957:Models, Genetic; D008958:Models, Molecular; D009690:Nucleic Acid Conformation; D011485:Protein Binding; D017434:Protein Structure, Tertiary
chemical_list: D001426:Bacterial Proteins; D004268:DNA-Binding Proteins; D004247:DNA; D004265:DNA Helicases
keywords: DNA repair; DNA replication; mutation; recombination; transcription