PICH: A DNA Translocase Specially Adapted for Processing Anaphase Bridge DNA

Research output: Contribution to journalJournal articleResearchpeer-review

  • A. Biebricher
  • S. Hirano
  • J. Enzlin
  • N. Wiechens
  • W. Streicher
  • D. Huttner
  • L.H-C. Wang
  • E. Nigg
  • T. Owen-Hughes
  • Liu, Ying
  • E. Peterman
  • G. Wuite
  • Hickson, Ian David
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.
Original languageEnglish
JournalMolecular Cell
Issue number5
Pages (from-to)691-701
Number of pages11
Publication statusPublished - 12 Sep 2013

    Research areas

  • Adenosine Triphosphate, Anaphase, Animals, Chromatids, DNA Helicases, Humans, Microscopy, Fluorescence, Nucleic Acid Heteroduplexes, Nucleosomes, Protein Transport, Recombinant Proteins

ID: 88641264