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pubmed:abstractText |
DNA helicases catalyze the unwinding of double-stranded (ds) DNA to yield the single-stranded (ss) DNA intermediates required in DNA replication, recombination, and repair. DNA helicases couple the free energy of nucleoside triphosphate (NTP) binding and hydrolysis to separate the two complementary DNA strands while also translocating vectorially along the DNA substrate. As such, helicases are functionally DNA motor proteins. The functional form of helicases generally appears to be oligomeric (usually dimers or hexamers), which provides the helicase with multiple DNA binding sites that are required for translocation and DNA unwinding. The affinity of ss- versus dsDNA for these multiple DNA binding sites is modulated allosterically by NTP binding, hydrolysis, and product release, which is central to helicase-catalyzed DNA unwinding. The mechanistic details of the DNA unwinding, translocation, and NTPase reactions are only starting to emerge. We discuss energy coupling by DNA helicases in general, and by the dimeric E. coli Rep helicase in particular, focusing on the similarities of these enzymes to classical motor proteins.
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