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Science. 2013 Apr 19;340(6130):353-6. doi: 10.1126/science.1231122.

The helicase-like domains of type III restriction enzymes trigger long-range diffusion along DNA.

Author information

1
DNA motors group, Biotechnology Center, Technische Universität Dresden, 01062 Dresden, Germany.

Abstract

Helicases are ubiquitous adenosine triphosphatases (ATPases) with widespread roles in genome metabolism. Here, we report a previously undescribed functionality for ATPases with helicase-like domains; namely, that ATP hydrolysis can trigger ATP-independent long-range protein diffusion on DNA in one dimension (1D). Specifically, using single-molecule fluorescence microscopy we show that the Type III restriction enzyme EcoP15I uses its ATPase to switch into a distinct structural state that diffuses on DNA over long distances and long times. The switching occurs only upon binding to the target site and requires hydrolysis of ~30 ATPs. We define the mechanism for these enzymes and show how ATPase activity is involved in DNA target site verification and 1D signaling, roles that are common in DNA metabolism: for example, in nucleotide excision and mismatch repair.

PMID:
23599494
PMCID:
PMC3646237
DOI:
10.1126/science.1231122
[Indexed for MEDLINE]
Free PMC Article
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