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Specialized interfaces of Smc5/6 control hinge stability and DNA association

Alt, Aaron ; Dang, Hung Q ; Wells, Owen S ; Polo, Luis M ; Smith, Matt A ; McGregor, Grant A ; Welte, Thomas ; Lehmann, Alan R ; Pearl, Laurence H ; Murray, Johanne M ; Oliver, Antony W

Nature communications, 2017-01, Vol.8 (1), p.14011-14, Article 14011 [Revista revisada por pares]

England: Nature Publishing Group

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Specialized interfaces of Smc5/6 control hinge stability and DNA association
Autor: Alt, Aaron ; Dang, Hung Q ; Wells, Owen S ; Polo, Luis M ; Smith, Matt A ; McGregor, Grant A ; Welte, Thomas ; Lehmann, Alan R ; Pearl, Laurence H ; Murray, Johanne M ; Oliver, Antony W
Materias: Adenosine Triphosphatases - chemistry ; Binding Sites ; Cell Cycle Proteins - chemistry ; Cell Cycle Proteins - genetics ; Cell Cycle Proteins - metabolism ; Cell Line, Tumor ; Cell Survival - physiology ; Chromosomal Proteins, Non-Histone - chemistry ; Chromosomal Proteins, Non-Histone - genetics ; Chromosomal Proteins, Non-Histone - metabolism ; Chromosomes ; Cohesins ; Crystallography, X-Ray ; DNA Damage ; DNA Repair - physiology ; DNA, Single-Stranded - metabolism ; DNA-Binding Proteins - chemistry ; Genomes ; Humans ; Life sciences ; Models, Molecular ; Multiprotein Complexes - chemistry ; Mutagenesis, Site-Directed ; Mutation ; Phenotype ; Protein Binding ; Protein Domains - physiology ; Protein Multimerization - physiology ; Proteins ; Recombinant Proteins - chemistry ; Recombinant Proteins - genetics ; Recombinant Proteins - metabolism ; Schizosaccharomyces - physiology ; Schizosaccharomyces pombe Proteins - chemistry ; Schizosaccharomyces pombe Proteins - genetics ; Schizosaccharomyces pombe Proteins - metabolism ; Yeast
Es parte de: Nature communications, 2017-01, Vol.8 (1), p.14011-14, Article 14011
Descripción: The Structural Maintenance of Chromosomes (SMC) complexes: cohesin, condensin and Smc5/6 are involved in the organization of higher-order chromosome structure-which is essential for accurate chromosome duplication and segregation. Each complex is scaffolded by a specific SMC protein dimer (heterodimer in eukaryotes) held together via their hinge domains. Here we show that the Smc5/6-hinge, like those of cohesin and condensin, also forms a toroidal structure but with distinctive subunit interfaces absent from the other SMC complexes; an unusual 'molecular latch' and a functional 'hub'. Defined mutations in these interfaces cause severe phenotypic effects with sensitivity to DNA-damaging agents in fission yeast and reduced viability in human cells. We show that the Smc5/6-hinge complex binds preferentially to ssDNA and that this interaction is affected by both 'latch' and 'hub' mutations, suggesting a key role for these unique features in controlling DNA association by the Smc5/6 complex.
Editor: England: Nature Publishing Group
Idioma: Inglés

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Specialized interfaces of Smc5/6 control hinge stability and DNA association

Alt, Aaron ; Dang, Hung Q ; Wells, Owen S ; Polo, Luis M ; Smith, Matt A ; McGregor, Grant A ; Welte, Thomas ; Lehmann, Alan R ; Pearl, Laurence H ; Murray, Johanne M ; Oliver, Antony W

England: Nature Publishing Group

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