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

Friedrich W Schwarz, Júlia Tóth, Kara van Aelst, Guanshen Cui, Sylvia Clausing, Mark D Szczelkun, Ralf Seidel

Research output: Contribution to journalArticle (Academic Journal)peer-review

48 Citations (Scopus)

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.
Original languageEnglish
Pages (from-to)353-6
Number of pages4
JournalScience
Volume340
Issue number6130
DOIs
Publication statusPublished - 19 Apr 2013

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