TY - JOUR
T1 - The helicase-like domains of type III restriction enzymes trigger long-range diffusion along DNA
AU - Schwarz, Friedrich W
AU - Tóth, Júlia
AU - van Aelst, Kara
AU - Cui, Guanshen
AU - Clausing, Sylvia
AU - Szczelkun, Mark D
AU - Seidel, Ralf
PY - 2013/4/19
Y1 - 2013/4/19
N2 - 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.
AB - 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.
U2 - 10.1126/science.1231122
DO - 10.1126/science.1231122
M3 - Article (Academic Journal)
C2 - 23599494
SN - 0036-8075
VL - 340
SP - 353
EP - 356
JO - Science
JF - Science
IS - 6130
ER -