3N7N

Structure of Csm1/Lrs4 complex

3N7N の概要

• エントリーDOI: 10.2210/pdb3n7n/pdb
• 関連するPDBエントリー: 3N4R 3N4S 3N4X
• 分子名称: Monopolin complex subunit CSM1, Monopolin complex subunit LRS4 (2 entities in total)
• 機能のキーワード: meiosis, rdna, replication
• 由来する生物種: Saccharomyces cerevisiae (brewer's yeast,lager beer yeast,yeast); 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 109587.11

構造登録者

Corbett, K.D.,Harrison, S.C. (登録日: 2010-05-27, 公開日: 2010-09-01, 最終更新日: 2024-02-21)

主引用文献

Corbett, K.D.,Yip, C.K.,Ee, L.S.,Walz, T.,Amon, A.,Harrison, S.C.
The Monopolin Complex Crosslinks Kinetochore Components to Regulate Chromosome-Microtubule Attachments.
Cell(Cambridge,Mass.), 142:556-567, 2010

PubMed Abstract: The monopolin complex regulates different types of kinetochore-microtubule attachments in fungi, ensuring sister chromatid co-orientation in Saccharomyces cerevisiae meiosis I and inhibiting merotelic attachment in Schizosaccharomyces pombe mitosis. In addition, the monopolin complex maintains the integrity and silencing of ribosomal DNA (rDNA) repeats in the nucleolus. We show here that the S. cerevisiae Csm1/Lrs4 monopolin subcomplex has a distinctive V-shaped structure, with two pairs of protein-protein interaction domains positioned approximately 10 nm apart. Csm1 presents a conserved hydrophobic surface patch that binds two kinetochore proteins: Dsn1, a subunit of the outer-kinetochore MIND/Mis12 complex, and Mif2/CENP-C. Csm1 point-mutations that disrupt kinetochore-subunit binding also disrupt sister chromatid co-orientation in S. cerevisiae meiosis I. We further show that the same Csm1 point-mutations affect rDNA silencing, probably by disrupting binding to the rDNA-associated protein Tof2. We propose that Csm1/Lrs4 functions as a molecular clamp, crosslinking kinetochore components to enforce sister chromatid co-orientation in S. cerevisiae meiosis I and to suppress merotelic attachment in S. pombe mitosis, and crosslinking rDNA repeats to aid rDNA silencing.

PubMed: 20723757
DOI: 10.1016/j.cell.2010.07.017

実験手法

X-RAY DIFFRACTION (3.9 Å)