3N7N
Structure of Csm1/Lrs4 complex
Summary for 3N7N
Entry DOI | 10.2210/pdb3n7n/pdb |
Related | 3N4R 3N4S 3N4X |
Descriptor | Monopolin complex subunit CSM1, Monopolin complex subunit LRS4 (2 entities in total) |
Functional Keywords | meiosis, rdna, replication |
Biological source | Saccharomyces cerevisiae (brewer's yeast,lager beer yeast,yeast) More |
Total number of polymer chains | 6 |
Total formula weight | 109587.11 |
Authors | Corbett, K.D.,Harrison, S.C. (deposition date: 2010-05-27, release date: 2010-09-01, Last modification date: 2024-02-21) |
Primary citation | 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 Cited by 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: 20723757DOI: 10.1016/j.cell.2010.07.017 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.9 Å) |
Structure validation
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