- SMC protein
SMC proteins represent a large family of
ATPasesthat participate in many aspects of higher-order chromosome organization and dynamics.cite journal |author=Hirano T|title=The ABCs of SMC proteins: two-armed ATPases for chromosome condensation, cohesion, and repair|journal= Genes Dev |volume= 16 |issue= 4 |pages= 399–414 |year= 2002| doi = 10.1101/gad.955102 |pmid= 11850403] cite journal |author=Hirano T|title=SMC proteins and chromosome mechanics: from bacteria to humans|journal= Philos Trans R Soc Lond B Biol Sci |volume= 360 |issue= 1455 |pages= 507–14 |year= 2005| doi = 10.1098/rstb.2004.1606 |pmid= 15897176] cite journal |author=Huang CE, Milutinovich M, Koshland D|title=Rings, bracelet or snaps: fashionable alternatives for Smc complexes|journal= Philos Trans R Soc Lond B Biol Sci |volume= 360 |issue= 1455 |pages= 537–42 |year= 2005| doi = 10.1098/rstb.2004.1609 |pmid= 15897179] SMC stands for Structural Maintenance of Chromosomes.
SMC proteins are conserved from bacteria to humans. Most bacteria have a single SMC protein in individual species that forms a homodimer. In a subclass of
Gram-negativebacteria including Escherichia coli, a distantly related protein known as MukB plays an equivalent role.
Eukaryotes have at least six SMC proteins in individual organisms, and they form three distinct heterodimers with specialized functions:
* A pair of SMC1 and SMC3 constitutes the core subunits of the
cohesincomplexes involved in sister chromatid cohesion.
* Likewise, a pair of SMC2 and SMC4 acts as the core of the
condensincomplexes implicated in chromosome condensation.
* A dimer composed of SMC5 and SMC6 functions as part of a yet-to-be-named octameric complex implicated in
DNA repairand checkpoint responses.
Each complex contains a distinct set of non-SMC regulatory subunits.
Some organisms have variants of SMC proteins. For instance, mammals have a
meiosis-specific variant of SMC1, known as SMC1β. The nematode Caenorhabditis eleganshas an SMC4-variant that has a specialized role in dosage compensation.
SMC protein monomers have a modular structure and contain the following domains:
*1) Walker A
*3) hinge region
*4) coiled-coil region II
*5) Walker B ATP-binding motif
SMC dimers form a V-shaped molecule with two long
coiled-coilarms, each having an ATP-binding domain at its distal end. The ATP-binding domain of SMC proteins is structurally related to that of ABC transporters, a large family of transmembrane proteins that actively transport small molecules across cellular membranes. It is thought that the cycle of ATP binding and hydrolysismodulates the cycle of closing and opening of the V-shaped molecule, but the detailed mechanisms of action of SMC proteins remain to be determined.
*, Gene|SMC1B, Gene|SMC2, Gene|SMC3, Gene|SMC4, Gene|SMC5, Gene|SMC6
Cornelia de Lange Syndrome
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NCAPH2 — Non SMC condensin II complex, subunit H2 Identifiers Symbols NCAPH2; CAPH2; MGC15858; MGC18000; MGC2455; MGC4133; MGC5305; MGC8640 External IDs … Wikipedia
NCAPD2 — Non SMC condensin I complex, subunit D2 Identifiers Symbols NCAPD2; CAP D2; CNAP1; KIAA0159; hCAP D2 External IDs … Wikipedia
NCAPH — Non SMC condensin I complex, subunit H Identifiers Symbols NCAPH; BRRN1; CAP H; HCAP H External IDs … Wikipedia
NCAPG — Non SMC condensin I complex, subunit G Identifiers Symbols NCAPG; CAPG; CHCG; FLJ12450; HCAP G; MGC126525; NY MEL 3 External IDs … Wikipedia
NCAPD3 — Non SMC condensin II complex, subunit D3 Identifiers Symbols NCAPD3; CAP D3; FLJ42888; KIAA0056; MGC104671; hCAP D3; hHCP 6; hcp 6 External IDs … Wikipedia