title: Rings, bracelet or snaps: fashionable alternatives for Smc complexes.
abstract: The mechanism of higher order chromosome organization has eluded researchers for over 100 years. A breakthrough occurred with the discovery of multi-subunit protein complexes that contain a core of two molecules from the structural maintenance of chromosome (Smc) family. Smc complexes are important structural components of chromosome organization in diverse aspects of DNA metabolism, including sister chromatid cohesion, condensation, global gene repression, DNA repair and homologous recombination. In these different processes, Smc complexes may facilitate chromosome organization by tethering together two parts of the same or different chromatin strands. The mechanism of tethering by Smc complexes remains to be elucidated, but a number of intriguing topological alternatives are suggested by the unusual structural features of Smc complexes, including their large coiled-coil domains and ATPase activities. Distinguishing between these possibilities will require innovative new approaches.
authors.affiliation: Department of Embryology, Carnegie Institution of Washington, 115 W. University Parkway, Baltimore, MD 21210, USA.
authors.forename: Catherine E
authors.initials: CE
authors.lastname: Huang
authors.forename: Mark
authors.initials: M
authors.lastname: Milutinovich
authors.forename: Douglas
authors.initials: D
authors.lastname: Koshland
mesh_terms: D000251:Adenosine Triphosphatases / Q000378:metabolism / Q000502:physiology*; D001426:Bacterial Proteins / Q000378:metabolism / Q000502:physiology*; D002453:Cell Cycle / Q000502:physiology*; D018797:Cell Cycle Proteins / Q000378:metabolism / Q000502:physiology*; D002842:Chromatids / Q000378:metabolism / Q000502:physiology*; D002868:Chromosomal Proteins, Non-Histone; D004268:DNA-Binding Proteins / Q000378:metabolism / Q000502:physiology*; D005057:Eukaryotic Cells / Q000502:physiology*; D005656:Fungal Proteins; D008954:Models, Biological; D046912:Multiprotein Complexes / Q000378:metabolism / Q000502:physiology*; D009687:Nuclear Proteins / Q000378:metabolism / Q000502:physiology*; D000097722:Cohesins
chemical_list: D000251:Adenosine Triphosphatases; D001426:Bacterial Proteins; D018797:Cell Cycle Proteins; D002868:Chromosomal Proteins, Non-Histone; D004268:DNA-Binding Proteins; D005656:Fungal Proteins; D046912:Multiprotein Complexes; D009687:Nuclear Proteins; D000097722:Cohesins; C118650:SMC protein, Bacteria; C108312:condensin complexes