Abstract
Helicases are motor proteins that move unidirectionally on nucleic acids by deriving energy from concerted and coordinated NTP hydrolysis reaction. A class of helicases, ring shaped hexameric helicases, plays essential roles in DNA replication, repair, recombination, and transcription. Owing to their shape, ring shaped hexameric helicases can encircle single or double-stranded nucleic acid and unwind double-stranded DNA or promote branch migration reaction on Holliday junctions. We discuss the organization and structure of bacterial and eukaryotic hexameric helicases that are involved in DNA replication, focusing on the mechanism of DNA binding, coordinated NTP hydrolysis, and coupling of NTP hydrolysis to translocation and DNA strand separation. We also discuss the synergy between helicase and the DNA polymerase activities at the replication fork in the replisome.
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