| Monopolin complex subunit CSM1 | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| Organism | |||||||
| Symbol | CSM1 | ||||||
| Entrez | 850447 | ||||||
| RefSeq (mRNA) | NM_001178792 | ||||||
| RefSeq (Prot) | NP_010009 | ||||||
| UniProt | P25651 | ||||||
| Other data | |||||||
| Chromosome | III: 0.26 - 0.26 Mb | ||||||
| |||||||
| Casein kinase I homolog HRR25 | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| Organism | |||||||
| Symbol | HRR25 | ||||||
| Entrez | 855897 | ||||||
| RefSeq (mRNA) | NM_001184018 | ||||||
| RefSeq (Prot) | NP_015120 | ||||||
| UniProt | P29295 | ||||||
| Other data | |||||||
| EC number | 2.7.11.1 | ||||||
| Chromosome | XVI: 0.16 - 0.17 Mb | ||||||
| |||||||
| Monopolin complex subunit LRS4 | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| Organism | |||||||
| Symbol | LRS4 | ||||||
| Entrez | 852049 | ||||||
| RefSeq (mRNA) | NM_001180747 | ||||||
| RefSeq (Prot) | NP_010727 | ||||||
| UniProt | Q04087 | ||||||
| Other data | |||||||
| Chromosome | IV: 1.34 - 1.34 Mb | ||||||
| |||||||
| Monopolin complex subunit MAM1 | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| Organism | |||||||
| Symbol | MAM1 | ||||||
| Entrez | 856843 | ||||||
| RefSeq (mRNA) | NM_001178997 | ||||||
| RefSeq (Prot) | NP_011032 | ||||||
| UniProt | P40065 | ||||||
| Other data | |||||||
| Chromosome | V: 0.37 - 0.37 Mb | ||||||
| |||||||
Monopolin is a protein complex that in budding yeast is composed of the four proteins CSM1, HRR25, LRS4, and MAM1. Monopolin is required for the segregation of homologous centromeres to opposite poles of a dividing cell during anaphase I of meiosis.[1] This occurs by bridging DSN1 kinetochore proteins to sister kinetochores within the centromere to physically fuse them and allow for the microtubules to pull each homolog toward opposite mitotic spindles.[2]
Molecular structure
Monopolin is composed of a 4 CSM1:2 LRS4 complex which forms a V-shaped structure with two globular heads at the ends, which are responsible for directly crosslinking sister kinetochores.[1] Bound to each CSM1 head is a MAM1 protein which recruits one copy of the HRR25 kinase.[3] The hydrophobic cavity on the CSM1 subunit allows the hydrophobic regions of Monopolin receptor and kinetochore protein, DSN1, to bind to and fuse the sister kinetochores.[2] Microtubules can then attach to the kinetochores on the homologous centromeres and pull them toward opposite mitotic spindles to complete anaphase of meiosis I.
References
- 1 2 Corbett KD, Yip CK, Ee LS, Walz T, Amon A, Harrison SC (August 2010). "The monopolin complex crosslinks kinetochore components to regulate chromosome-microtubule attachments". Cell. 142 (4): 556–67. doi:10.1016/j.cell.2010.07.017. PMC 2955198. PMID 20723757.
- 1 2 Plowman, Rebecca; Singh, Namit; Tromer, Eelco C.; Payan, Angel; Duro, Eris; Spanos, Christos; Rappsilber, Juri; Snel, Berend; Kops, Geert J. P.L.; Corbett, Kevin D.; Marston, Adele L. (2019-09-01). "The molecular basis of monopolin recruitment to the kinetochore". Chromosoma. 128 (3): 331–354. doi:10.1007/s00412-019-00700-0. ISSN 1432-0886. PMC 6823300. PMID 31037469.
- ↑ Corbett, Kevin D.; Harrison, Stephen C. (2012-06-28). "Molecular Architecture of the Yeast Monopolin Complex". Cell Reports. 1 (6): 583–589. doi:10.1016/j.celrep.2012.05.012. ISSN 2211-1247. PMC 3494995. PMID 22813733.