5YRQ

Crystal structure of Rad5 and Rev1

5YRQ の概要

• エントリーDOI: 10.2210/pdb5yrq/pdb
• 関連するPDBエントリー: 2ABC
• 分子名称: DNA repair protein RAD5,DNA repair protein REV1 (2 entities in total)
• 機能のキーワード: rad5, dna damage tolerance, e3 ligase, tls polymerase, rev1, dna binding protein
• 由来する生物種: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 67813.26

構造登録者

Chen, Z.C.,Zhou, C.Y. (登録日: 2017-11-09, 公開日: 2019-03-20, 最終更新日: 2024-03-27)

主引用文献

Xu, X.,Lin, A.Y.,Zhou, C.Y.,Blackwell, S.R.,Zhang, Y.R.,Wang, Z.H.,Feng, Q.Q.,Guan, R.F.,Hanna, M.D.,Chen, Z.C.,Xiao, W.
Involvement of budding yeast Rad5 in translesion DNA synthesis through physical interaction with Rev1.
Nucleic Acids Res., 44:5231-5245, 2016

PubMed Abstract: DNA damage tolerance (DDT) is responsible for genomic stability and cell viability by bypassing the replication block. In Saccharomyces cerevisiae DDT employs two parallel branch pathways to bypass the DNA lesion, namely translesion DNA synthesis (TLS) and error-free lesion bypass, which are mediated by sequential modifications of PCNA. Rad5 has been placed in the error-free branch of DDT because it contains an E3 ligase domain required for PCNA polyubiquitination. Rad5 is a multi-functional protein and may also play a role in TLS, since it interacts with the TLS polymerase Rev1. In this study we mapped the Rev1-interaction domain in Rad5 to the amino acid resolution and demonstrated that Rad5 is indeed involved in TLS possibly through recruitment of Rev1. Genetic analyses show that the dual functions of Rad5 can be separated and reconstituted. Crystal structure analysis of the Rad5-Rev1 interaction reveals a consensus RFF motif in the Rad5 N-terminus that binds to a hydrophobic pocket within the C-terminal domain of Rev1 that is highly conserved in eukaryotes. This study indicates that Rad5 plays a critical role in pathway choice between TLS and error-free DDT.

PubMed: 27001510
DOI: 10.1093/nar/gkw183

実験手法

X-RAY DIFFRACTION (1.999 Å)