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Additional recommended knowledge
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-negative bacteria 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:
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 elegans has an SMC4-variant that has a specialized role in dosage compensation.
SMC protein monomers have a modular structure and contain the following domains:
SMC dimers form a V-shaped molecule with two long coiled-coil arms, 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 hydrolysis modulates the cycle of closing and opening of the V-shaped molecule, but the detailed mechanisms of action of SMC proteins remain to be determined.
|This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "SMC_protein". A list of authors is available in Wikipedia.|