A novel TPR-BEN domain interaction mediates PICH-BEND3 association

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

Standard

A novel TPR-BEN domain interaction mediates PICH-BEND3 association. / Pitchai, Ganesha P; Kaulich, Manuel; Bizard, Anna H; Mesa, Pablo; Yao, Qi; Sarlos, Kata; Streicher, Werner W; Nigg, Erich A; Montoya, Guillermo; Hickson, Ian D.

In: Nucleic Acids Research, Vol. 19, No. 2, 2017, p. 11413–11424.

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

Harvard

Pitchai, GP, Kaulich, M, Bizard, AH, Mesa, P, Yao, Q, Sarlos, K, Streicher, WW, Nigg, EA, Montoya, G & Hickson, ID 2017, 'A novel TPR-BEN domain interaction mediates PICH-BEND3 association', Nucleic Acids Research, vol. 19, no. 2, pp. 11413–11424. https://doi.org/10.1093/nar/gkx792

APA

Pitchai, G. P., Kaulich, M., Bizard, A. H., Mesa, P., Yao, Q., Sarlos, K., Streicher, W. W., Nigg, E. A., Montoya, G., & Hickson, I. D. (2017). A novel TPR-BEN domain interaction mediates PICH-BEND3 association. Nucleic Acids Research, 19(2), 11413–11424. https://doi.org/10.1093/nar/gkx792

Vancouver

Pitchai GP, Kaulich M, Bizard AH, Mesa P, Yao Q, Sarlos K et al. A novel TPR-BEN domain interaction mediates PICH-BEND3 association. Nucleic Acids Research. 2017;19(2):11413–11424. https://doi.org/10.1093/nar/gkx792

Author

Pitchai, Ganesha P ; Kaulich, Manuel ; Bizard, Anna H ; Mesa, Pablo ; Yao, Qi ; Sarlos, Kata ; Streicher, Werner W ; Nigg, Erich A ; Montoya, Guillermo ; Hickson, Ian D. / A novel TPR-BEN domain interaction mediates PICH-BEND3 association. In: Nucleic Acids Research. 2017 ; Vol. 19, No. 2. pp. 11413–11424.

Bibtex

@article{9ba4058cf9834e4db429b0855d2ca5ec,
title = "A novel TPR-BEN domain interaction mediates PICH-BEND3 association",
abstract = "PICH is a DNA translocase required for the maintenance of chromosome stability in human cells. Recent data indicate that PICH co-operates with topoisomerase IIα to suppress pathological chromosome missegregation through promoting the resolution of ultra-fine anaphase bridges (UFBs). Here, we identify the BEN domain-containing protein 3 (BEND3) as an interaction partner of PICH in human cells in mitosis. We have purified full length PICH and BEND3 and shown that they exhibit a functional biochemical interaction in vitro. We demonstrate that the PICH-BEND3 interaction occurs via a novel interface between a TPR domain in PICH and a BEN domain in BEND3, and have determined the crystal structure of this TPR-BEN complex at 2.2 {\AA} resolution. Based on the structure, we identified amino acids important for the TPR-BEN domain interaction, and for the functional interaction of the full-length proteins. Our data reveal a proposed new function for BEND3 in association with PICH, and the first example of a specific protein-protein interaction mediated by a BEN domain.",
keywords = "Journal Article",
author = "Pitchai, {Ganesha P} and Manuel Kaulich and Bizard, {Anna H} and Pablo Mesa and Qi Yao and Kata Sarlos and Streicher, {Werner W} and Nigg, {Erich A} and Guillermo Montoya and Hickson, {Ian D}",
note = "{\textcopyright} The Author(s) 2017. Published by Oxford University Press on behalf of Nucleic Acids Research.",
year = "2017",
doi = "10.1093/nar/gkx792",
language = "English",
volume = "19",
pages = "11413–11424",
journal = "Nucleic Acids Research",
issn = "0305-1048",
publisher = "Oxford University Press",
number = "2",

}

RIS

TY - JOUR

T1 - A novel TPR-BEN domain interaction mediates PICH-BEND3 association

AU - Pitchai, Ganesha P

AU - Kaulich, Manuel

AU - Bizard, Anna H

AU - Mesa, Pablo

AU - Yao, Qi

AU - Sarlos, Kata

AU - Streicher, Werner W

AU - Nigg, Erich A

AU - Montoya, Guillermo

AU - Hickson, Ian D

N1 - © The Author(s) 2017. Published by Oxford University Press on behalf of Nucleic Acids Research.

PY - 2017

Y1 - 2017

N2 - PICH is a DNA translocase required for the maintenance of chromosome stability in human cells. Recent data indicate that PICH co-operates with topoisomerase IIα to suppress pathological chromosome missegregation through promoting the resolution of ultra-fine anaphase bridges (UFBs). Here, we identify the BEN domain-containing protein 3 (BEND3) as an interaction partner of PICH in human cells in mitosis. We have purified full length PICH and BEND3 and shown that they exhibit a functional biochemical interaction in vitro. We demonstrate that the PICH-BEND3 interaction occurs via a novel interface between a TPR domain in PICH and a BEN domain in BEND3, and have determined the crystal structure of this TPR-BEN complex at 2.2 Å resolution. Based on the structure, we identified amino acids important for the TPR-BEN domain interaction, and for the functional interaction of the full-length proteins. Our data reveal a proposed new function for BEND3 in association with PICH, and the first example of a specific protein-protein interaction mediated by a BEN domain.

AB - PICH is a DNA translocase required for the maintenance of chromosome stability in human cells. Recent data indicate that PICH co-operates with topoisomerase IIα to suppress pathological chromosome missegregation through promoting the resolution of ultra-fine anaphase bridges (UFBs). Here, we identify the BEN domain-containing protein 3 (BEND3) as an interaction partner of PICH in human cells in mitosis. We have purified full length PICH and BEND3 and shown that they exhibit a functional biochemical interaction in vitro. We demonstrate that the PICH-BEND3 interaction occurs via a novel interface between a TPR domain in PICH and a BEN domain in BEND3, and have determined the crystal structure of this TPR-BEN complex at 2.2 Å resolution. Based on the structure, we identified amino acids important for the TPR-BEN domain interaction, and for the functional interaction of the full-length proteins. Our data reveal a proposed new function for BEND3 in association with PICH, and the first example of a specific protein-protein interaction mediated by a BEN domain.

KW - Journal Article

U2 - 10.1093/nar/gkx792

DO - 10.1093/nar/gkx792

M3 - Journal article

C2 - 28977671

VL - 19

SP - 11413

EP - 11424

JO - Nucleic Acids Research

JF - Nucleic Acids Research

SN - 0305-1048

IS - 2

ER -

ID: 184290286