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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Vydané v:	Nature structural & molecular biology Ročník 26; číslo 3; s. 227 - 236
Hlavní autori:	Bürmann, Frank, Lee, Byung-Gil, Than, Thane, Sinn, Ludwig, O'Reilly, Francis J, Yatskevich, Stanislau, Rappsilber, Juri, Hu, Bin, Nasmyth, Kim, Löwe, Jan
Médium:	Journal Article
Jazyk:	English
Vydavateľské údaje:	United States Nature Publishing Group 01.03.2019
Predmet:	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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Abstract	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.
AbstractList	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. 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.Two evolutionarily distant SMC–kleisin complexes are shown to contain a bendable coiled-coil discontinuity near the middle of their arms, which permits a folded conformation with potential implications for DNA loading and translocation. 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.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.
Author	Than, Thane Sinn, Ludwig Yatskevich, Stanislau Hu, Bin Rappsilber, Juri Nasmyth, Kim Löwe, Jan Lee, Byung-Gil Bürmann, Frank O'Reilly, Francis J
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Snippet	Structural maintenance of chromosomes (SMC)-kleisin complexes organize chromosomal DNAs in all domains of life, with key roles in chromosome segregation, DNA... Structural maintenance of chromosomes (SMC)–kleisin complexes organize chromosomal DNAs in all domains of life, with key roles in chromosome segregation, DNA...
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SubjectTerms	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
Title	A folded conformation of MukBEF and cohesin
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