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| Subject Categories: Cell Cycle | Structural Biology |
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| The EMBO Journal
(2007) 26, 4413–4422, doi:10.1038/sj.emboj.7601864 Published online 27 September 2007 |
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| Structural analysis of the ParR/parC plasmid partition complex |
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| Jakob Møller-Jensen1, 4, Simon Ringgaard2, Christopher P Mercogliano1, Kenn Gerdes3 and Jan Löwe1 |
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1 MRC-Laboratory of Molecular Biology, Cambridge, UK 2 Department of Biochemistry and Molecular Biology, University of Southern Denmark, Odense M, Denmark 3 Institute for Cell and Molecular Biosciences, Newcastle University, Newcastle upon Tyne, UK 4 Present address: Department of Biochemistry and Molecular Biology, University of Southern Denmark, Campusvej 55, Odense M 5230, Denmark To whom correspondence should be addressed Jakob Møller-Jensen, Department of Biochemistry and Molecular Biology, University of Southern Denmark, Campusvej 55, Odense M 5230, Denmark. Tel.: +45 6550 2423; Fax: +45 6550 2467; E-mail: jakobm@bmb.sdu.dk Jan Löwe, MRC-Laboratory of Molecular Biology, Hills Road, Cambridge CB2 0QH, UK. Tel.: +44 1223 252969; Fax: +44 1223 213556; E-mail: jyl@mrc-lmb.cam.ac.uk Received 9 February 2007; Accepted 31 August 2007; Published online 27 September 2007. |
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| Abstract |
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| Accurate DNA partition at cell division is vital to all living organisms. In bacteria, this process can involve partition loci, which are found on both chromosomes and plasmids. The initial step in Escherichia coli plasmid R1 partition involves the formation of a partition complex between the DNA-binding protein ParR and its cognate centromere site parC on the DNA. The partition complex is recognized by a second partition protein, the actin-like ATPase ParM, which forms filaments required for the active bidirectional movement of DNA replicates. Here, we present the 2.8 Å crystal structure of ParR from E. coli plasmid pB171. ParR forms a tight dimer resembling a large family of dimeric ribbon–helix–helix (RHH)2 site-specific DNA-binding proteins. Crystallographic and electron microscopic data further indicate that ParR dimers assemble into a helix structure with DNA-binding sites facing outward. Genetic and biochemical experiments support a structural arrangement in which the centromere-like parC DNA is wrapped around a ParR protein scaffold. This structure holds implications for how ParM polymerization drives active DNA transport during plasmid partition. |
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| Keywords: centromere, DNA segregation, ParR, partition complex, plasmid |
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Top of page MORE ARTICLES LIKE THISThese links to content published by NPG are automatically generated RESEARCHStructural analysis of the ParR/parC plasmid partition complex The EMBO Journal Article Bacterial actin: architecture of the ParMRC plasmid DNA partitioning complex The EMBO Journal Article Segrosome structure revealed by a complex of ParR with centromere DNA Nature Letters to Editor (20 Dec 2007) |
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