Biophysical characterization of the interaction between FAAP20‐UBZ4 domain and Rev1‐BRCT domain. Issue 20 (28th August 2015)

• Record Type: Journal Article
• Authors: Lim, Kyungeun; Lee, Mi-Kyung; Duong, Phuong T.M.; Liu, Dinan; Sung, Sieun; Choi, Byong-Seok
• Is Part Of: FEBS letters. Volume 589:Issue 20(2015) Part B
• Page Start: 3037
• Page End: 3043
• Publication Date: 2015-08-28
• Subjects: FA -- Fanconi anemia -- ICL -- interstrand cross-link -- DSB -- double-strand break -- HR -- homologous recombination -- MMC -- mitomycin C -- DEB -- diepoxybutane -- TLS -- translesion synthesis -- NER -- nucleotide excision repair -- FAAP20 -- Fanconi anemia-associated protein 20 -- UBZ4 -- ubiquitin-binding zinc finger 4 -- BRCT -- BRCA1 C-terminus -- PBS -- phosphate-buffered saline -- ITC -- isothermal titration calorimetry -- TEV -- tobacco etch virus -- Fanconi anemia pathway -- Interstrand cross-link -- Fanconi anemia-associated protein 20 -- Rev1 -- Ubiquitin -- Nuclear magnetic resonance; Biochemistry -- Periodicals; Biophysics -- Periodicals; Molecular biology -- Periodicals; Biochimie -- Périodiques; Biochemistry; Biophysics; Molecular biology; Periodicals; 572.05
• DOI: 10.1016/j.febslet.2015.08.021
• Languages: English
• ISSNs: 0014-5793

Abstract

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. Abstract : The CSP mapping showed FAAP20 has distinct binding surfaces for ubiquitin and Rev1. FAAP20‐UBZ4 interacts with ubiquitin through the C‐terminal α‐helix and tail. UBZ4 bound to ubiquitin interacts with Rev1‐BRCT through the same C‐terminal tail. We suggest a mechanism by which FAAP20 recognizes Rev1 during ICL repair.