Biophysical characterization of the interaction between FAAP20-UBZ4 domain and Rev1-BRCT domain

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Title
Biophysical characterization of the interaction between FAAP20-UBZ4 domain and Rev1-BRCT domain
Author(s)
K Lim; Mi Kyung Lee; P T M Duong; D Liu; S Sung; B S Choi
Bibliographic Citation
FEBS Letters, vol. 589, no. 20, pp. 3037-3043
Publication Year
2015
Abstract
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.
Keyword
Fanconi anemia pathwayFanconi anemia-associated protein 20Interstrand cross-linkNuclear magnetic resonanceRev1Ubiquitin
ISSN
0014-5793
Publisher
Wiley
DOI
http://dx.doi.org/10.1016/j.febslet.2015.08.021
Type
Article
Appears in Collections:
Division of Biomedical Research > Disease Target Structure Research Center > 1. Journal Articles
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