Biophysical characterization of the interaction between FAAP20-UBZ4 domain and Rev1-BRCT domain
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- 作者：Kyungeun Lima ; Mi-Kyung Leeb ; Phuong T.M. Duonga ; Dinan Liua ; Sieun Sunga ; Byong-Seok Choia ; byongseok.choi@kaist.ac.kr" class="auth_mail" title="E-mail the corresponding author
- 关键词：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
- 刊名：FEBS Letters
- 出版年：2015
- 出版时间：7 October 2015
- 年：2015
- 卷：589
- 期：20
- 页码：3037-3043
- 全文大小：1728 K
文摘
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The CSP mapping showed FAAP20 has distinct binding surfaces for ubiquitin and Rev1.
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FAAP20-UBZ4 interacts with ubiquitin through the C-terminal 伪-helix and tail.
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UBZ4 bound to ubiquitin interacts with Rev1-BRCT through the same C-terminal tail.
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We suggest a mechanism by which FAAP20 recognizes Rev1 during ICL repair.