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Curr Opin Chem Biol. 2011 Oct;15(5):595-605. doi: 10.1016/j.cbpa.2011.08.003. Epub 2011 Aug 22.

Dynamic coupling between the motors of DNA replication: hexameric helicase, DNA polymerase, and primase.

Author information

1
UMDNJ-Robert Wood Johnson Medical School, Piscataway, NJ, USA. patelss@umdnj.edu

Abstract

Helicases are molecular motor proteins that couple NTP hydrolysis to directional movement along nucleic acids. A class of helicases characterized by their ring-shaped hexameric structures translocate processively and unidirectionally along single-stranded (ss) DNA to separate the strands of double-stranded (ds) DNA, aiding both in the initiation and fork progression during DNA replication. These replicative ring-shaped helicases are found from virus to human. We review recent biochemical and structural studies that have expanded our understanding on how hexameric helicases use the NTPase reaction to translocate on ssDNA, unwind dsDNA, and how their physical and functional interactions with the DNA polymerase and primase enzymes coordinate replication of the two strands of dsDNA.

PMID:
21865075
PMCID:
PMC3189298
DOI:
10.1016/j.cbpa.2011.08.003
[Indexed for MEDLINE]
Free PMC Article

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