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Biophysical characterization of the interaction between FAAP20‐UBZ4 domain and Rev1‐BRCT domain
Author(s) -
Lim Kyungeun,
Lee Mi-Kyung,
Duong Phuong T.M.,
Liu Dinan,
Sung Sieun,
Choi Byong-Seok
Publication year - 2015
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2015.08.021
Subject(s) - domain (mathematical analysis) , characterization (materials science) , chemistry , biophysics , computational biology , nanotechnology , biology , materials science , mathematics , mathematical analysis
FAAP20 (Fanconi anemia‐associated protein 20) is a subunit of the Fanconi anemia (FA) core complex that repairs interstrand cross‐links. To understand the molecular basis for the FA core complex‐mediated recruitment of Rev1 to the DNA lesion, we characterized the interactions among FAAP20‐UBZ4, Rev1‐BRCT, and ubiquitin using NMR. We found that FAAP20‐UBZ4 binds not only ubiquitin but also Rev1‐BRCT. Mapping the protein–protein interactions showed that FAAP20‐UBZ4 has distinct binding surfaces for ubiquitin and Rev1‐BRCT. In addition, the chemical exchange patterns indicated that the interaction between FAAP20‐UBZ4 and ubiquitin might enhance the binding affinity between FAAP20‐UBZ4 and Rev1‐BRCT. These results provide new insight into the Rev1 recognition mechanism by FAAP20.