Condensin: Difference between revisions
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<StructureSection load=' | <StructureSection load='5oqn' size='340' side='right' caption='Yeast SMC subunit 2 (green) and subunit 3 (grey) complex with DNA (PDB code [[5oqn]]' scene=''> | ||
== Function == | == Function == | ||
'''Condensin''' or '''structural maintenance of chromosome protein''' (SMC) is required for correctly package and divide the cell's genome. SMC uses ATP to affect conformational changes in DNA, to correct DNA compaction, organization and segregation<ref>PMID:28181049</ref>. SMC exhibits the ability to super-coil DNA<ref>PMID:23218009</ref>. SMC of ''E. coli'' is named '''MukB''' or '''Chromosome partition protein A'''. SMC is found in species from bacteria to human. SMC and cohesin which share structural similarities, are essential for separting the genome into daughter cells during cell division. SMC reorganizes chromsomes into their compact mitotic structure while cohesin glues replicated sister chromatids together until they split at anaphase<ref>PMID:12838344</ref>. | '''Condensin''' or '''structural maintenance of chromosome protein''' (SMC) is required for correctly package and divide the cell's genome. SMC uses ATP to affect conformational changes in DNA, to correct DNA compaction, organization and segregation<ref>PMID:28181049</ref>. SMC exhibits the ability to super-coil DNA<ref>PMID:23218009</ref>. SMC of ''E. coli'' is named '''MukB''' or '''Chromosome partition protein A'''. '''MukE''' and '''MukF''' are associated with MukB. SMC is found in species from bacteria to human. SMC and cohesin which share structural similarities, are essential for separting the genome into daughter cells during cell division. SMC reorganizes chromsomes into their compact mitotic structure while cohesin glues replicated sister chromatids together until they split at anaphase<ref>PMID:12838344</ref>. | ||
== Relevance == | == Relevance == | ||
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== Structural highlights == | == Structural highlights == | ||
SMC is a multisubunit complex. In vertebrates condensin complex is formed from the association of SMC2 and SMC4 subunits. SMC2 and SMC4 contain 3 domains: head domain forming | SMC is a multisubunit complex. In vertebrates condensin complex is formed from the association of SMC2 and SMC4 subunits. SMC2 and SMC4 contain 3 domains: head domain forming an ATPase, a long coiled-coil region and a hinge domain which facilitates SMC2/SMC4 dimerization. | ||
</StructureSection> | </StructureSection> | ||
Latest revision as of 10:31, 4 April 2020
FunctionCondensin or structural maintenance of chromosome protein (SMC) is required for correctly package and divide the cell's genome. SMC uses ATP to affect conformational changes in DNA, to correct DNA compaction, organization and segregation[1]. SMC exhibits the ability to super-coil DNA[2]. SMC of E. coli is named MukB or Chromosome partition protein A. MukE and MukF are associated with MukB. SMC is found in species from bacteria to human. SMC and cohesin which share structural similarities, are essential for separting the genome into daughter cells during cell division. SMC reorganizes chromsomes into their compact mitotic structure while cohesin glues replicated sister chromatids together until they split at anaphase[3]. RelevanceSMC plays important role in human disease and bacterial pathogenicity and its inhibitors are studied for therapeutic purposes[4]. Mutations or removal of SMC subunits cause errors in chromosome segregation and likely cell death. Structural highlightsSMC is a multisubunit complex. In vertebrates condensin complex is formed from the association of SMC2 and SMC4 subunits. SMC2 and SMC4 contain 3 domains: head domain forming an ATPase, a long coiled-coil region and a hinge domain which facilitates SMC2/SMC4 dimerization.
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3D Structures of condensin3D Structures of condensin
Updated on 04-April-2020
ReferencesReferences
- ↑ Kalitsis P, Zhang T, Marshall KM, Nielsen CF, Hudson DF. Condensin, master organizer of the genome. Chromosome Res. 2017 Mar;25(1):61-76. doi: 10.1007/s10577-017-9553-0. Epub 2017, Feb 9. PMID:28181049 doi:http://dx.doi.org/10.1007/s10577-017-9553-0
- ↑ Thadani R, Uhlmann F, Heeger S. Condensin, chromatin crossbarring and chromosome condensation. Curr Biol. 2012 Dec 4;22(23):R1012-21. doi: 10.1016/j.cub.2012.10.023. PMID:23218009 doi:http://dx.doi.org/10.1016/j.cub.2012.10.023
- ↑ Hagstrom KA, Meyer BJ. Condensin and cohesin: more than chromosome compactor and glue. Nat Rev Genet. 2003 Jul;4(7):520-34. doi: 10.1038/nrg1110. PMID:12838344 doi:http://dx.doi.org/10.1038/nrg1110
- ↑ Zhao H, Petrushenko ZM, Walker JK, Baudry J, Zgurskaya HI, Rybenkov VV. Small Molecule Condensin Inhibitors. ACS Infect Dis. 2018 Dec 14;4(12):1737-1745. doi: 10.1021/acsinfecdis.8b00222., Epub 2018 Oct 22. PMID:30346684 doi:http://dx.doi.org/10.1021/acsinfecdis.8b00222