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PICH: a DNA translocase specially adapted for processing anaphase bridge DNA
Andreas Biebricher1, Seiki Hirano2, Jacqueline H Enzlin3
1LaserLaB Amsterdam and Department of Physics, VU University Amsterdam, De Boelelaan 1081, 1081HV Amsterdam, The Netherlands.
Molecular Cell
|August 27, 2013
Summary
The Plk1-interacting checkpoint helicase (PICH) protein stabilizes DNA under tension at ultrafine anaphase bridges (UFBs) during cell division. This DNA binding and stabilization by PICH aids in resolving entangled sister chromatids, ensuring proper cell replication.
Area of Science:
- Molecular Biology
- Cell Biology
- Biophysics
Background:
- The Plk1-interacting checkpoint helicase (PICH) protein is found at ultrafine anaphase bridges (UFBs) with DNA repair proteins like BLM.
- The precise function of PICH and its recruitment mechanism to UFBs remain largely uncharacterized.
Purpose of the Study:
- To investigate the biophysical properties and function of PICH in an in vitro model of anaphase bridges.
Main Methods:
- Utilized microfluidics, fluorescence microscopy, and optical tweezers to study PICH-DNA interactions.
- Developed an in vitro model simulating anaphase bridge conditions.
Main Results:
- PICH exhibits high-affinity binding to duplex DNA, with ATP-dependent translocation and DNA extension.
- PICH DNA-binding affinity increases with tension-induced DNA stretching, mimicking mitotic spindle forces on UFBs.
- PICH binding appears to reduce force-induced DNA melting.
Conclusions:
- PICH functions to recognize and stabilize stretched DNA under tension during anaphase.
- This stabilization mechanism likely facilitates the resolution of entangled sister chromatids at UFBs.
- PICH plays a crucial role in mitotic checkpoint and genome stability.
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