Structural analysis of the ParR/parC plasmid partition complex

Jakob Moller-Jensen; Simon Ringgaard; Christopher P. Mercogliano; Kenn Gerdes; Jan Loewe

doi:10.1038/sj.emboj.7601864

Structural analysis of the ParR/parC plasmid partition complex

Jakob Moller-Jensen, Simon Ringgaard, Christopher P. Mercogliano, Kenn Gerdes, Jan Loewe

55 Citationer (Scopus)

Abstract

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 2.8A 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.

Originalsprog	Engelsk
Tidsskrift	E M B O Journal
Vol/bind	26
Udgave nummer	20
Sider (fra-til)	4413-4422
Antal sider	10
ISSN	0261-4189
DOI	https://doi.org/10.1038/sj.emboj.7601864
Status	Udgivet - 2007
Udgivet eksternt	Ja

Adgang til dokumentet

10.1038/sj.emboj.7601864

Citationsformater

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title = "Structural analysis of the ParR/parC plasmid partition complex",

abstract = "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 2.8A 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.",

author = "Jakob Moller-Jensen and Simon Ringgaard and Mercogliano, {Christopher P.} and Kenn Gerdes and Jan Loewe",

year = "2007",

doi = "10.1038/sj.emboj.7601864",

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TY - JOUR

T1 - Structural analysis of the ParR/parC plasmid partition complex

AU - Moller-Jensen, Jakob

AU - Ringgaard, Simon

AU - Mercogliano, Christopher P.

AU - Gerdes, Kenn

AU - Loewe, Jan

PY - 2007

Y1 - 2007

N2 - 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 2.8A 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.

AB - 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 2.8A 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.

U2 - 10.1038/sj.emboj.7601864

DO - 10.1038/sj.emboj.7601864

M3 - Journal article

C2 - 17898804

SN - 0261-4189

VL - 26

SP - 4413

EP - 4422

JO - E M B O Journal

JF - E M B O Journal

IS - 20

ER -