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

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PICH : A DNA Translocase Specially Adapted for Processing Anaphase Bridge DNA. / Biebricher, A.; Hirano, S.; Enzlin, J.; Wiechens, N.; Streicher, W.; Huttner, D.; Wang, L.H-C.; Nigg, E.; Owen-Hughes, T.; Liu, Y.; Peterman, E.; Wuite, G.; Hickson, I.

In: Molecular Cell, Vol. 51, No. 5, 12.09.2013, p. 691-701.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Biebricher, A, Hirano, S, Enzlin, J, Wiechens, N, Streicher, W, Huttner, D, Wang, LH-C, Nigg, E, Owen-Hughes, T, Liu, Y, Peterman, E, Wuite, G & Hickson, I 2013, 'PICH: A DNA Translocase Specially Adapted for Processing Anaphase Bridge DNA', Molecular Cell, vol. 51, no. 5, pp. 691-701. https://doi.org/10.1016/j.molcel.2013.07.016

APA

Biebricher, A., Hirano, S., Enzlin, J., Wiechens, N., Streicher, W., Huttner, D., ... Hickson, I. (2013). PICH: A DNA Translocase Specially Adapted for Processing Anaphase Bridge DNA. Molecular Cell, 51(5), 691-701. https://doi.org/10.1016/j.molcel.2013.07.016

Vancouver

Biebricher A, Hirano S, Enzlin J, Wiechens N, Streicher W, Huttner D et al. PICH: A DNA Translocase Specially Adapted for Processing Anaphase Bridge DNA. Molecular Cell. 2013 Sep 12;51(5):691-701. https://doi.org/10.1016/j.molcel.2013.07.016

Author

Biebricher, A. ; Hirano, S. ; Enzlin, J. ; Wiechens, N. ; Streicher, W. ; Huttner, D. ; Wang, L.H-C. ; Nigg, E. ; Owen-Hughes, T. ; Liu, Y. ; Peterman, E. ; Wuite, G. ; Hickson, I. / PICH : A DNA Translocase Specially Adapted for Processing Anaphase Bridge DNA. In: Molecular Cell. 2013 ; Vol. 51, No. 5. pp. 691-701.

Bibtex

@article{9cd97c35e0674e278ead21dd590a9cc5,
title = "PICH: A DNA Translocase Specially Adapted for Processing Anaphase Bridge DNA",
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 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.",
keywords = "Adenosine Triphosphate, Anaphase, Animals, Chromatids, DNA Helicases, Humans, Microscopy, Fluorescence, Nucleic Acid Heteroduplexes, Nucleosomes, Protein Transport, Recombinant Proteins",
author = "A. Biebricher and S. Hirano and J. Enzlin and N. Wiechens and W. Streicher and D. Huttner and L.H-C. Wang and E. Nigg and T. Owen-Hughes and Y. Liu and E. Peterman and G. Wuite and I. Hickson",
note = "Copyright {\circledC} 2013 Elsevier Inc. All rights reserved.",
year = "2013",
month = "9",
day = "12",
doi = "10.1016/j.molcel.2013.07.016",
language = "English",
volume = "51",
pages = "691--701",
journal = "Molecular Cell",
issn = "1097-2765",
publisher = "Cell Press",
number = "5",

}

RIS

TY - JOUR

T1 - PICH

T2 - A DNA Translocase Specially Adapted for Processing Anaphase Bridge DNA

AU - Biebricher, A.

AU - Hirano, S.

AU - Enzlin, J.

AU - Wiechens, N.

AU - Streicher, W.

AU - Huttner, D.

AU - Wang, L.H-C.

AU - Nigg, E.

AU - Owen-Hughes, T.

AU - Liu, Y.

AU - Peterman, E.

AU - Wuite, G.

AU - Hickson, I.

N1 - Copyright © 2013 Elsevier Inc. All rights reserved.

PY - 2013/9/12

Y1 - 2013/9/12

N2 - 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.

AB - 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.

KW - Adenosine Triphosphate

KW - Anaphase

KW - Animals

KW - Chromatids

KW - DNA Helicases

KW - Humans

KW - Microscopy, Fluorescence

KW - Nucleic Acid Heteroduplexes

KW - Nucleosomes

KW - Protein Transport

KW - Recombinant Proteins

UR - http://www.scopus.com/inward/record.url?scp=84883825487&partnerID=8YFLogxK

U2 - 10.1016/j.molcel.2013.07.016

DO - 10.1016/j.molcel.2013.07.016

M3 - Journal article

C2 - 23973328

AN - SCOPUS:84883825487

VL - 51

SP - 691

EP - 701

JO - Molecular Cell

JF - Molecular Cell

SN - 1097-2765

IS - 5

ER -

ID: 88641264