3T7I

Crystal structure of Se-Met Rtt107p (residues 820-1070)

3T7I の概要

• エントリーDOI: 10.2210/pdb3t7i/pdb
• 関連するPDBエントリー: 3T7J 3T7K
• 分子名称: Regulator of Ty1 transposition protein 107 (2 entities in total)
• 機能のキーワード: brct, dna repair, phospho-peptide, protein binding
• 由来する生物種: Saccharomyces cerevisiae (yeast)
• 細胞内の位置: Nucleus : P38850
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 59129.97

構造登録者

Li, X.,Li, F.,Wu, J.,Shi, Y. (登録日: 2011-07-30, 公開日: 2012-02-15, 最終更新日: 2024-11-20)

主引用文献

Li, X.,Liu, K.,Li, F.,Wang, J.,Huang, H.,Wu, J.,Shi, Y.
Structure of C-terminal Tandem BRCT Repeats of Rtt107 Protein Reveals Critical Role in Interaction with Phosphorylated Histone H2A during DNA Damage Repair
J.Biol.Chem., 287:9137-9146, 2012

PubMed Abstract: Rtt107 (regulator of Ty1 transposition 107; Esc4) is a DNA repair protein from Saccharomyces cerevisiae that can restore stalled replication forks following DNA damage. There are six BRCT (BRCA1 C-terminal) domains in Rtt107 that act as binding sites for other recruited proteins during DNA repair. Several Rtt107 binding partners have been identified, including Slx4, Rtt101, Rad55, and the Smc5/6 (structural maintenance of chromosome) protein complex. Rtt107 can reportedly be recruited to chromatin in the presence of Rtt101 and Rtt109 upon DNA damage, but the chromatin-binding site of Rtt107 has not been identified. Here, we report our investigation of the interaction between phosphorylated histone H2A (γH2A) and the C-terminal tandem BRCT repeats (BRCT(5)-BRCT(6)) of Rtt107. The crystal structures of BRCT(5)-BRCT(6) alone and in a complex with γH2A reveal the molecular basis of the Rtt107-γH2A interaction. We used in vitro mutagenesis and a fluorescence polarization assay to confirm the location of the Rtt107 motif that is crucial for this interaction. In addition, these assays indicated that this interaction requires the phosphorylation of H2A. An in vivo phenotypic analysis in yeast demonstrated the critical role of BRCT(5)-BRCT(6) and its interaction with γH2A during the DNA damage response. Our results shed new light on the molecular mechanism by which Rtt107 is recruited to chromatin in response to stalled DNA replication forks.

PubMed: 22262834
DOI: 10.1074/jbc.M111.311860

実験手法

X-RAY DIFFRACTION (2.3 Å)