Condensins are large protein complexes that play a central role in chromosome assembly and segregation during mitosis and meiosis. The core subunits condensins (SMC2 and SMC4) are conserved among all eukaryotic species that have been studied to date. The non-SMC subunits unique to condensin I are also conserved among eukaryotes, but the occurrence of the non-SMC subunits unique to condensin II is highly variable among species. Condensins are multisubunit protein complexes that play a fundamental role in the structural and functional organization of chromosomes in the three domains of life. Most eukaryotic species have two different types of condensin complexes, known as condensins I and II, that fulfill nonoverlapping functions and are subjected to differential regulation during mitosis and meiosis. Recent studies revealed that the two complexes contribute to a wide variety of interphase chromosome functions, such as gene regulation, recombination, and repair. Also emerging are their cell type- and tissue-specific functions and relevance to human disease. Biochemical and structural analyses of eukaryotic and bacterial condensins steadily uncover the mechanisms of action of this class of highly sophisticated molecular machines.
Condensin complex entraps the bases of a DNA loop transiently in two separate chambers. Single-molecule imaging and cryo-electron microscopy suggest a putative power-stroke movement at the first chamber that feeds DNA into the SMC-kleisin ring upon adenosine triphosphate binding, whereas the second chamber holds on upstream of the same DNA double helix. Here you can see a cryoEM structure of the Condensin peripheral Ycg1 subcomplex bound to DNA isolated from Saccharomyces cereviseae (PDB code: 7QFW)
#molecularart ... #immolecular ... #condensin ... #chromosome ... #yeast ... #DNA ... #complex ... #cryoem
Structure of the condensin-DNA complex rendered with @proteinimaging and depicted with @corelphotopaint
Condensin complex entraps the bases of a DNA loop transiently in two separate chambers. Single-molecule imaging and cryo-electron microscopy suggest a putative power-stroke movement at the first chamber that feeds DNA into the SMC-kleisin ring upon adenosine triphosphate binding, whereas the second chamber holds on upstream of the same DNA double helix. Here you can see a cryoEM structure of the Condensin peripheral Ycg1 subcomplex bound to DNA isolated from Saccharomyces cereviseae (PDB code: 7QFW)
#molecularart ... #immolecular ... #condensin ... #chromosome ... #yeast ... #DNA ... #complex ... #cryoem
Structure of the condensin-DNA complex rendered with @proteinimaging and depicted with @corelphotopaint
