PICH: A DNA Translocase Specially Adapted for Processing Anaphase Bridge DNA
Research output: Contribution to journal › Journal article › Research › peer-review
Standard
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 journal › Journal article › Research › peer-review
Harvard
APA
Vancouver
Author
Bibtex
}
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