PICH acts as a force-dependent nucleosome remodeler

Dian Spakman, Tinka V. M. Clement, Andreas S. Biebricher, Graeme A. King, Manika I. Singh, Ian D. Hickson, Erwin J. G. Peterman () and Gijs J. L. Wuite ()
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Dian Spakman: Vrije Universiteit Amsterdam
Tinka V. M. Clement: Vrije Universiteit Amsterdam
Andreas S. Biebricher: Vrije Universiteit Amsterdam
Graeme A. King: Vrije Universiteit Amsterdam
Manika I. Singh: University of Copenhagen
Ian D. Hickson: University of Copenhagen
Erwin J. G. Peterman: Vrije Universiteit Amsterdam
Gijs J. L. Wuite: Vrije Universiteit Amsterdam

Nature Communications, 2022, vol. 13, issue 1, 1-12

Abstract: Abstract In anaphase, any unresolved DNA entanglements between the segregating sister chromatids can give rise to chromatin bridges. To prevent genome instability, chromatin bridges must be resolved prior to cytokinesis. The SNF2 protein PICH has been proposed to play a direct role in this process through the remodeling of nucleosomes. However, direct evidence of nucleosome remodeling by PICH has remained elusive. Here, we present an in vitro single-molecule assay that mimics chromatin under tension, as is found in anaphase chromatin bridges. Applying a combination of dual-trap optical tweezers and fluorescence imaging of PICH and histones bound to a nucleosome-array construct, we show that PICH is a tension- and ATP-dependent nucleosome remodeler that facilitates nucleosome unwrapping and then subsequently slides remaining histones along the DNA. This work elucidates the role of PICH in chromatin-bridge dissolution, and might provide molecular insights into the mechanisms of related SNF2 proteins.

Date: 2022
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DOI: 10.1038/s41467-022-35040-8

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