An asymmetric SMC–kleisin bridge in prokaryotic condensin
| Autor: | Yeon-Gil Kim, Victor Giménez-Oya, Byung-Ha Oh, Young-Min Soh, Frank Bürmann, Ho-Chul Shin, Stephan Gruber, Jérôme Basquin |
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| Rok vydání: | 2013 |
| Předmět: |
Models
Molecular Protein Conformation Condensin Cell Cycle Proteins macromolecular substances Bacillus subtilis Crystallography X-Ray medicine.disease_cause DNA-binding protein 03 medical and health sciences chemistry.chemical_compound 0302 clinical medicine Protein structure Bacterial Proteins Structural Biology medicine Binding site Molecular Biology 030304 developmental biology Adenosine Triphosphatases Genetics 0303 health sciences Mutation Binding Sites biology biology.organism_classification Protein Structure Tertiary Cell biology DNA-Binding Proteins Establishment of sister chromatid cohesion Cross-Linking Reagents Streptococcus pneumoniae chemistry Multiprotein Complexes biology.protein Protein Multimerization 030217 neurology & neurosurgery DNA |
| Zdroj: | Nature Structural & Molecular Biology. 20:371-379 |
| ISSN: | 1545-9985 1545-9993 |
| DOI: | 10.1038/nsmb.2488 |
| Popis: | Eukaryotic structural maintenance of chromosomes (SMC)-kleisin complexes form large, ring-shaped assemblies that promote accurate chromosome segregation. Their asymmetric structural core comprises SMC heterodimers that associate with both ends of a kleisin subunit. However, prokaryotic condensin Smc-ScpAB is composed of symmetric Smc homodimers associated with the kleisin ScpA in a postulated symmetrical manner. Here, we demonstrate that Smc molecules have two distinct binding sites for ScpA. The N terminus of ScpA binds the Smc coiled coil, whereas the C terminus binds the Smc ATPase domain. We show that in Bacillus subtilis cells, an Smc dimer is bridged by a single ScpAB to generate asymmetric tripartite rings analogous to eukaryotic SMC complexes. We define a molecular mechanism that ensures asymmetric assembly, and we conclude that the basic architecture of SMC-kleisin rings evolved before the emergence of eukaryotes. |
| Databáze: | OpenAIRE |
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