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

Pitchai, Ganesha P. and Kaulich, Manuel and Bizard, Anna H. and Mesa, Pablo and Yao, Qi and Sarlos, Kata and Streicher, Werner W. and Nigg, Erich A. and Montoya, Guillermo and Hickson, Ian D.. (2017) A novel TPR-BEN domain interaction mediates PICH-BEND3 association. Nucleic Acids Research, 45 (19). p. 12.

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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.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Former Organization Units Biozentrum > Cell Biology (Nigg)
UniBasel Contributors:Nigg, Erich A.
Item Type:Article, refereed
Article Subtype:Research Article
Publisher:Oxford University Press
Note:Publication type according to Uni Basel Research Database: Journal article
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Last Modified:16 May 2018 06:38
Deposited On:16 May 2018 06:38

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