Biophysical characterization of the interaction between FAAP20-UBZ4 domain and Rev1-BRCT domain.
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.
Mesh Terms:
Amino Acid Sequence, Binding Sites, Biophysical Processes, Fanconi Anemia Complementation Group Proteins, Humans, Magnetic Resonance Spectroscopy, Models, Molecular, Molecular Sequence Data, Nuclear Proteins, Nucleotidyltransferases, Protein Binding, Protein Interaction Mapping, Protein Structure, Tertiary, Sequence Homology, Amino Acid, Surface Properties, Ubiquitin
Amino Acid Sequence, Binding Sites, Biophysical Processes, Fanconi Anemia Complementation Group Proteins, Humans, Magnetic Resonance Spectroscopy, Models, Molecular, Molecular Sequence Data, Nuclear Proteins, Nucleotidyltransferases, Protein Binding, Protein Interaction Mapping, Protein Structure, Tertiary, Sequence Homology, Amino Acid, Surface Properties, Ubiquitin
FEBS Lett.
Date: Oct. 07, 2015
PubMed ID: 26318859
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