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  An asymmetric SMC-kleisin bridge in prokaryotic condensin

Bürmann, F., Shin, H.-C., Basquin, J., Soh, Y.-M., Giménez-Oya, V., Kim, Y.-G., et al. (2013). An asymmetric SMC-kleisin bridge in prokaryotic condensin. NATURE STRUCTURAL & MOLECULAR BIOLOGY, 20(3), 371-379. doi:10.1038/nsmb.2488.

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 Creators:
Bürmann, Frank1, Author              
Shin, Ho-Chul2, Author
Basquin, Jerome3, Author              
Soh, Young-Min2, Author
Giménez-Oya, Victor1, Author              
Kim, Yeon-Gil2, Author
Oh, Byung-Ha2, Author
Gruber, Stephan1, Author              
Affiliations:
1Gruber, Stephan / Chromosome Organization and Dynamics, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565151              
2external, ou_persistent22              
3Conti, Elena / Structural Cell Biology, Max Planck Institute of Biochemistry, Max Planck Society, ou_1565144              

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Free keywords: PROMOTES CHROMOSOME SEGREGATION; SISTER-CHROMATID COHESION; ESCHERICHIA-COLI; BACILLUS-SUBTILIS; ATP HYDROLYSIS; DNA; PROTEINS; COMPLEX; ARCHITECTURE; BACTERIAL
 Abstract: 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 sub fills 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.

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Language(s): eng - English
 Dates: 2013-03
 Publication Status: Published in print
 Pages: 9
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: ISI: 000316041000020
DOI: 10.1038/nsmb.2488
 Degree: -

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Title: NATURE STRUCTURAL & MOLECULAR BIOLOGY
Source Genre: Journal
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Publ. Info: 75 VARICK ST, 9TH FLR, NEW YORK, NY 10013-1917 USA : NATURE PUBLISHING GROUP
Pages: - Volume / Issue: 20 (3) Sequence Number: - Start / End Page: 371 - 379 Identifier: ISSN: 1545-9993