Journal
MOLECULAR CELL
Volume 51, Issue 5, Pages 691-701Publisher
CELL PRESS
DOI: 10.1016/j.molcel.2013.07.016
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Funding
- Cancer Research (UK)
- Nordea Foundation (Denmark)
- Association for International Cancer Research (UK)
- Danish Cancer Society
- Novo Nordisk Foundation (Denmark)
- LaserLab Europe
- University of Basel (Switzerland)
- VICI of NWO
- ERC
- Worldwide Cancer Research [10-0500] Funding Source: researchfish
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The Plk1-interacting checkpoint helicase (PICH) protein localizes to ultrafine anaphase bridges (UFBs) in mitosis alongside a complex of DNA repair proteins, including the Bloom's syndrome protein (BLM). However, very little is known about the function of PICH or how it is recruited to UFBs. Using a combination of microfluidics, fluorescence microscopy, and optical tweezers, we have defined the properties of PICH in an in vitro model of an anaphase bridge. We show that PICH binds with a remarkably high affinity to duplex DNA, resulting in ATP-dependent protein translocation and extension of the DNA. Most strikingly, the affinity of PICH for binding DNA increases with tension-induced DNA stretching, which mimics the effect of the mitotic spindle on a UFB. PICH binding also appears to diminish force-induced DNA melting. We propose a model in which PICH recognizes and stabilizes DNA under tension during anaphase, thereby facilitating the resolution of entangled sister chromatids.
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