PICH acts as a force-dependent nucleosome remodeler

Research output: Contribution to journal › Journal article › Research › peer-review

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PICH acts as a force-dependent nucleosome remodeler. / Spakman, Dian; Clement, Tinka V.M.; Biebricher, Andreas S.; King, Graeme A.; Singh, Manika I.; Hickson, Ian D.; Peterman, Erwin J.G.; Wuite, Gijs J.L.

In: Nature Communications, Vol. 13, 7277, 2022.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Spakman, D, Clement, TVM, Biebricher, AS, King, GA, Singh, MI, Hickson, ID, Peterman, EJG & Wuite, GJL 2022, 'PICH acts as a force-dependent nucleosome remodeler', Nature Communications, vol. 13, 7277. https://doi.org/10.1038/s41467-022-35040-8

APA

Spakman, D., Clement, T. V. M., Biebricher, A. S., King, G. A., Singh, M. I., Hickson, I. D., Peterman, E. J. G., & Wuite, G. J. L. (2022). PICH acts as a force-dependent nucleosome remodeler. Nature Communications, 13, [7277]. https://doi.org/10.1038/s41467-022-35040-8

Vancouver

Spakman D, Clement TVM, Biebricher AS, King GA, Singh MI, Hickson ID et al. PICH acts as a force-dependent nucleosome remodeler. Nature Communications. 2022;13. 7277. https://doi.org/10.1038/s41467-022-35040-8

Author

Spakman, Dian ; Clement, Tinka V.M. ; Biebricher, Andreas S. ; King, Graeme A. ; Singh, Manika I. ; Hickson, Ian D. ; Peterman, Erwin J.G. ; Wuite, Gijs J.L. / PICH acts as a force-dependent nucleosome remodeler. In: Nature Communications. 2022 ; Vol. 13.

Bibtex

@article{f1e4e169d328464fbe751c08281ea6ea,

title = "PICH acts as a force-dependent nucleosome remodeler",

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.",

author = "Dian Spakman and Clement, {Tinka V.M.} and Biebricher, {Andreas S.} and King, {Graeme A.} and Singh, {Manika I.} and Hickson, {Ian D.} and Peterman, {Erwin J.G.} and Wuite, {Gijs J.L.}",

note = "Publisher Copyright: {\textcopyright} 2022, The Author(s).",

year = "2022",

doi = "10.1038/s41467-022-35040-8",

language = "English",

volume = "13",

journal = "Nature Communications",

issn = "2041-1723",

publisher = "nature publishing group",

}

RIS

TY - JOUR

T1 - PICH acts as a force-dependent nucleosome remodeler

AU - Spakman, Dian

AU - Clement, Tinka V.M.

AU - Biebricher, Andreas S.

AU - King, Graeme A.

AU - Singh, Manika I.

AU - Hickson, Ian D.

AU - Peterman, Erwin J.G.

AU - Wuite, Gijs J.L.

PY - 2022

Y1 - 2022

N2 - 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.

AB - 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.

U2 - 10.1038/s41467-022-35040-8

DO - 10.1038/s41467-022-35040-8

M3 - Journal article

C2 - 36433994

AN - SCOPUS:85142528777

VL - 13

JO - Nature Communications

JF - Nature Communications

SN - 2041-1723

M1 - 7277

ER -

ID: 330391020

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