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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.
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.
