Pitchai GP Kaulich M Bizard AH Mesa P Yao Q Sarlos K Streicher WW Nigg EA Montoya G Hickson ID 2017 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. application/pdf https://sonar.ch/global/documents/232510 eng info:eu-repo/semantics/altIdentifier/doi/10.1093/nar/gkx792 info:eu-repo/semantics/altIdentifier/pmid/28977671 info:eu-repo/semantics/openAccess Nucleic acids research. - 2017 Amino Acid Motifs Amino Acid Sequence Binding Sites Crystallography, X-Ray DNA Helicases HEK293 Cells HeLa Cells Humans Mitosis Models, Molecular Protein Binding Protein Domains Repressor Proteins Sequence Homology, Amino Acid A novel TPR-BEN domain interaction mediates PICH-BEND3 association. http://purl.org/coar/resource_type/c_6501