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

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Dokumenter

Ganesha P Pitchai, Manuel Kaulich, Anna H Bizard, Pablo Mesa, Qi Yao, Kata Sarlos, Werner W Streicher, Erich A Nigg, Guillermo Montoya, Ian D Hickson

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.

OriginalsprogEngelsk
TidsskriftNucleic Acids Research
Vol/bind19
Udgave nummer2
Sider (fra-til)11413–11424
ISSN0305-1048
DOI
StatusUdgivet - 2017

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