Projects per year
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 orhow it is recruited to UFBs. Using a combination of microfluidics, fluorescence microscopy, and optical tweezers, we have defined the properties of PICH in an invitro 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.
|Number of pages||11|
|Early online date||22 Aug 2013|
|Publication status||Published - 12 Sept 2013|
ASJC Scopus subject areas
- Molecular Biology
- Cell Biology
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- 2 Finished
Strategic Award: Wellcome Trust Technology Platform
Blow, J., Lamond, A. & Owen-Hughes, T.
1/01/13 → 30/09/18
Mechanisms for Remodelling Chromatin (Senior Fellowship Renewal)
1/01/12 → 31/05/19