Journal
SCIENCE
Volume 340, Issue 6130, Pages 353-356Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1231122
Keywords
-
Categories
Funding
- Wellcome Trust [084086]
- Deutsche Forschungsgemeinschaft (DFG) [SE 1646/1-1, SE 1646/7-1]
- European Research Council [261224]
- Dresden International Graduate School for Biomedicine and Bioengineering
- DFG
Ask authors/readers for more resources
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 similar to 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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available