5M1X

Crystal structure of S. cerevisiae Rfa1 N-OB domain mutant (K45E)

5M1X の概要

• エントリーDOI: 10.2210/pdb5m1x/pdb
• 分子名称: Replication factor A protein 1 (2 entities in total)
• 機能のキーワード: ob fold, replication
• 由来する生物種: Saccharomyces cerevisiae S288c (Baker's yeast)
• 細胞内の位置: Nucleus: P22336
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 62467.02

構造登録者

Seeber, A.,Hegnauer, A.M.,Hustedt, N.,Deshpande, I.,Poli, J.,Eglinger, J.,Pasero, P.,Gut, H.,Shinohara, M.,Hopfner, K.P.,Shimada, K.,Gasser, S.M. (登録日: 2016-10-11, 公開日: 2016-12-07, 最終更新日: 2024-10-23)

主引用文献

Seeber, A.,Hegnauer, A.M.,Hustedt, N.,Deshpande, I.,Poli, J.,Eglinger, J.,Pasero, P.,Gut, H.,Shinohara, M.,Hopfner, K.P.,Shimada, K.,Gasser, S.M.
RPA Mediates Recruitment of MRX to Forks and Double-Strand Breaks to Hold Sister Chromatids Together.
Mol. Cell, 64:951-966, 2016

PubMed Abstract: The Mre11-Rad50-Xrs2 (MRX) complex is related to SMC complexes that form rings capable of holding two distinct DNA strands together. MRX functions at stalled replication forks and double-strand breaks (DSBs). A mutation in the N-terminal OB fold of the 70 kDa subunit of yeast replication protein A, rfa1-t11, abrogates MRX recruitment to both types of DNA damage. The rfa1 mutation is functionally epistatic with loss of any of the MRX subunits for survival of replication fork stress or DSB recovery, although it does not compromise end-resection. High-resolution imaging shows that either the rfa1-t11 or the rad50Δ mutation lets stalled replication forks collapse and allows the separation not only of opposing ends but of sister chromatids at breaks. Given that cohesin loss does not provoke visible sister separation as long as the RPA-MRX contacts are intact, we conclude that MRX also serves as a structural linchpin holding sister chromatids together at breaks.

PubMed: 27889450
DOI: 10.1016/j.molcel.2016.10.032

実験手法

X-RAY DIFFRACTION (1.8 Å)