A novel TPR-BEN domain interaction mediates PICH-BEND3 association
JournalArticle (Originalarbeit in einer wissenschaftlichen Zeitschrift)
ID 3975106
Author(s) 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.
Author(s) at UniBasel Nigg, Erich
Year 2017
Title A novel TPR-BEN domain interaction mediates PICH-BEND3 association
Journal Nucleic Acids Research
Volume 45
Number 19
Pages / Article-Number 11413-11424
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 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.
Publisher Oxford University Press
ISSN/ISBN 0305-1048 ; 1362-4962
edoc-URL http://edoc.unibas.ch/56658/
Full Text on edoc Available
Digital Object Identifier DOI 10.1093/nar/gkx792
PubMed ID http://www.ncbi.nlm.nih.gov/pubmed/28977671
ISI-Number WOS:000414552300041
Document type (ISI) Article

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