期刊
EMBO JOURNAL
卷 30, 期 12, 页码 2364-2372出版社
WILEY
DOI: 10.1038/emboj.2011.141
关键词
ATP-dependent chromatin remodelling complex; DNA translocase; optical tweezers; step size
资金
- Alexandrine and Alexander L Sinsheimer Fund
- Kingsley Fund
- National Institutes of Health [GM60415]
- Howard Hughes Medical Institute
- [CA24014]
- [CA16056]
ATP-dependent chromatin remodelling complexes use the energy of ATP hydrolysis to reposition and reconfigure nucleosomes. Despite their diverse functions, all remodellers share highly conserved ATPase domains, many shown to translocate DNA. Understanding remodelling requires biophysical knowledge of the DNA translocation process: how the ATPase moves DNA and generates force, and how translocation and force generation are coupled on nucleosomes. Here, we characterize the real-time activity of a minimal RSC translocase 'motor' on bare DNA, using high-resolution optical tweezers and a 'tethered' translocase system. We observe on dsDNA a processivity of similar to 35 bp, a speed of similar to 25 bp/s, and a step size of 2.0 (+/-0.4, s.e.m.) bp. Surprisingly, the motor is capable of moving against high force, up to 30 pN, making it one of the most force-resistant motors known. We also provide evidence for DNA 'buckling' at initiation. These observations reveal the ATPase as a powerful DNA translocating motor capable of disrupting DNA-histone interactions by mechanical force. The EMBO Journal (2011) 30, 2364-2372. doi: 10.1038/emboj.2011.141; Published online 6 May 2011
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