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

Andreas Biebricher, Seiki Hirano, Jacqueline H. Enzlin, Nicola Wiechens, Werner W. Streicher, Diana Huttner, Lily H. C. Wang, Erich A. Nigg, Tom Owen-Hughes, Ying Liu, Erwin Peterman, Gijs J. L. Wuite, Ian D. Hickson (Lead / Corresponding author)

Research output: Contribution to journalArticle

52 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)691-701
Number of pages11
JournalMolecular Cell
Volume51
Issue number5
Early online date22 Aug 2013
DOIs
Publication statusPublished - 12 Sep 2013

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