A folded conformation of MukBEF and cohesin

Structural maintenance of chromosomes (SMC)-kleisin complexes organize chromosomal DNAs in all domains of life, with key roles in chromosome segregation, DNA repair and regulation of gene expression. They function through the entrapment and active translocation of DNA, but the underlying conformatio...

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Veröffentlicht in:Nature structural & molecular biology Jg. 26; H. 3; S. 227 - 236
Hauptverfasser: Bürmann, Frank, Lee, Byung-Gil, Than, Thane, Sinn, Ludwig, O'Reilly, Francis J, Yatskevich, Stanislau, Rappsilber, Juri, Hu, Bin, Nasmyth, Kim, Löwe, Jan
Format: Journal Article
Sprache:Englisch
Veröffentlicht: United States Nature Publishing Group 01.03.2019
Schlagworte:
Cell Cycle Proteins - metabolism
Chromosomal Proteins, Non-Histone - metabolism
Chromosomes
Cohesin
Cohesins
Coils
Conformation
Crosslinking
Deoxyribonucleic acid
Dimerization
Discontinuity
DNA
DNA repair
Domains
E coli
Elbow
Elbow (anatomy)
Entrapment
Escherichia coli
Escherichia coli Proteins - metabolism
Gene expression
Mass spectrometry
Mass spectroscopy
Protein Conformation
Protein Folding
Repressor Proteins - metabolism
Saccharomyces cerevisiae
Saccharomyces cerevisiae Proteins - metabolism
Translocation
ISSN:1545-9993, 1545-9985, 1545-9985
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Beschreibung
Zusammenfassung:Structural maintenance of chromosomes (SMC)-kleisin complexes organize chromosomal DNAs in all domains of life, with key roles in chromosome segregation, DNA repair and regulation of gene expression. They function through the entrapment and active translocation of DNA, but the underlying conformational changes are largely unclear. Using structural biology, mass spectrometry and cross-linking, we investigated the architecture of two evolutionarily distant SMC-kleisin complexes: MukBEF from Escherichia coli, and cohesin from Saccharomyces cerevisiae. We show that both contain a dynamic coiled-coil discontinuity, the elbow, near the middle of their arms that permits a folded conformation. Bending at the elbow brings into proximity the hinge dimerization domain and the head-kleisin module, situated at opposite ends of the arms. Our findings favour SMC activity models that include a large conformational change in the arms, such as a relative movement between DNA contact sites during DNA loading and translocation.
Bibliographie:ObjectType-Article-1
SourceType-Scholarly Journals-1
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ISSN:1545-9993
1545-9985
1545-9985
DOI:10.1038/s41594-019-0196-z