A novel TPR-BEN domain interaction mediates PICH-BEND3 association
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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.
I: Nucleic Acids Research, Bind 19, Nr. 2, 2017, s. 11413–11424.Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt
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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