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

TY - JOUR

T1 - PICH

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

AU - Biebricher, Andreas

AU - Hirano, Seiki

AU - Enzlin, Jacqueline H.

AU - Wiechens, Nicola

AU - Streicher, Werner W.

AU - Huttner, Diana

AU - Wang, Lily H. C.

AU - Nigg, Erich A.

AU - Owen-Hughes, Tom

AU - Liu, Ying

AU - Peterman, Erwin

AU - Wuite, Gijs J. L.

AU - Hickson, Ian D.

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 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.

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 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.

UR - https://www.scopus.com/pages/publications/84883825487

U2 - 10.1016/j.molcel.2013.07.016

DO - 10.1016/j.molcel.2013.07.016

M3 - Article

C2 - 23973328

AN - SCOPUS:84883825487

SN - 1097-2765

VL - 51

SP - 691

EP - 701

JO - Molecular Cell

JF - Molecular Cell

IS - 5

ER -