Partitioning of plasmid R1. The ParM protein exhibits ATPase activity and interacts with the centromere-like ParR-parC complex

Jensen, Rasmus Bugge; Gerdes, Kenn

doi:10.1006/jmbi.1997.1061

Cited by 112 publications

(115 citation statements)

References 38 publications

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“…Two plasmid molecules are paired by the binding of ParR to 10 direct repeats of parC, a cis-acting centromere-like DNA sequence (78). ParM (partitioning motor) is an ATPase that interacts with the ParRparC complex (77).…”

Section: The Actin-like Parm Protein and Plasmid-dna Segregationmentioning

confidence: 99%

The Bacterial Actin-Like Cytoskeleton

Carballido-López

2006

Microbiol Mol Biol Rev

177

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SUMMARY Recent advances have shown conclusively that bacterial cells possess distant but true homologues of actin (MreB, ParM, and the recently uncovered MamK protein). Despite weak amino acid sequence similarity, MreB and ParM exhibit high structural homology to actin. Just like F-actin in eukaryotes, MreB and ParM assemble into highly dynamic filamentous structures in vivo and in vitro. MreB-like proteins are essential for cell viability and have been implicated in major cellular processes, including cell morphogenesis, chromosome segregation, and cell polarity. ParM (a plasmid-encoded actin homologue) is responsible for driving plasmid-DNA partitioning. The dynamic prokaryotic actin-like cytoskeleton is thought to serve as a central organizer for the targeting and accurate positioning of proteins and nucleoprotein complexes, thereby (and by analogy to the eukaryotic cytoskeleton) spatially and temporally controlling macromolecular trafficking in bacterial cells. In this paper, the general properties and known functions of the actin orthologues in bacteria are reviewed.

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Section: The Actin-like Parm Protein and Plasmid-dna Segregationmentioning

confidence: 99%

The Bacterial Actin-Like Cytoskeleton

Carballido-López

2006

Microbiol Mol Biol Rev

177

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“…The locus includes three genes: parM codes for the actin-like ParM protein (M for motor); parC is the cis-acting centromeric DNA site (C for centromere); and parR (R for repressor) codes for the ParR protein, which binds to parC sequences and acts both to autoregulate transcription of the par genes and to link the ParM motor protein to the plasmid DNA. The parC site contains 10 iterons of 11-basepair repeats that act as sites for ParR binding (93).…”

Section: (I) Cytoskeletal Organization Of Mreb Proteins the Cellularmentioning

confidence: 99%

“…Filament assembly requires either ATP or a nonhydrolyzable ATP analog, indicating that the ATP-bound form of ParM is competent to polymerize (55,93,146). Unlike actin filaments, in which subunits are added only at one end of the filament, ParM filaments grow by addition of subunits at both ends of the growing polymer (55).…”

Section: (I) Cytoskeletal Organization Of Mreb Proteins the Cellularmentioning

confidence: 99%

The Bacterial Cytoskeleton

Shih

Rothfield

2006

Microbiol Mol Biol Rev

243

220

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SUMMARY In recent years it has been shown that bacteria contain a number of cytoskeletal structures. The bacterial cytoplasmic elements include homologs of the three major types of eukaryotic cytoskeletal proteins (actin, tubulin, and intermediate filament proteins) and a fourth group, the MinD-ParA group, that appears to be unique to bacteria. The cytoskeletal structures play important roles in cell division, cell polarity, cell shape regulation, plasmid partition, and other functions. The proteins self-assemble into filamentous structures in vitro and form intracellular ordered structures in vivo. In addition, there are a number of filamentous bacterial elements that may turn out to be cytoskeletal in nature. This review attempts to summarize and integrate the in vivo and in vitro aspects of these systems and to evaluate the probable future directions of this active research field.

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“…MreB is required for maintaining the shape of the cell and has also been implicated in chromosome segregation (Jones et al 2001;Defeu Soufo and Graumann 2005;Gitai et al 2005;Carballido-Lopez et al 2006). Other families of bacterial actins, such as ParM and AlfA, catalyze the segregation of plasmid DNA (Jensen and Gerdes 1997;Gerdes et al 2004;Becker et al 2006). ParM assembles two-stranded, actin-like filaments that display dynamic instability in vitro and is thought to function in vivo by polymerizing between newly replicated plasmids, pushing them apart (MollerJensen et al 2002(MollerJensen et al , 2003van den Ent et al 2002;Garner et al 2004Garner et al , 2007.…”

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confidence: 99%

Treadmilling of a prokaryotic tubulin-like protein, TubZ, required for plasmid stability in Bacillus thuringiensis

Larsen

Cusumano²,

Fujioka³

et al. 2007

Genes Dev.

178

218

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Prokaryotes rely on a distant tubulin homolog, FtsZ, for assembling the cytokinetic ring essential for cell division, but are otherwise generally thought to lack tubulin-like polymers that participate in processes such as DNA segregation. Here we characterize a protein (TubZ) from the Bacillus thuringiensis virulence plasmid pBtoxis, which is a member of the tubulin/FtsZ GTPase superfamily but is only distantly related to both FtsZ and tubulin. TubZ assembles dynamic, linear polymers that exhibit directional polymerization with plus and minus ends, movement by treadmilling, and a critical concentration for assembly. A point mutation (D269A) that alters a highly conserved catalytic residue within the T7 loop completely eliminates treadmilling and allows the formation of stable polymers at a much lower protein concentration than the wild-type protein.When expressed in trans, TubZ(D269A) coassembles with wild-type TubZ and significantly reduces the stability of pBtoxis, demonstrating a direct correlation between TubZ dynamics and plasmid maintenance. The tubZ gene is in an operon with tubR, which encodes a putative DNA-binding protein that regulates TubZ levels. Our results suggest that TubZ is representative of a novel class of prokaryotic cytoskeletal proteins important for plasmid stability that diverged long ago from the ancient tubulin/FtsZ ancestor.[Keywords: FtsZ; tubulin; cytoskeleton] Supplemental material is available at http://www.genesdev.org.

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Partitioning of plasmid R1. The ParM protein exhibits ATPase activity and interacts with the centromere-like ParR-parC complex

Cited by 112 publications

References 38 publications

The Bacterial Actin-Like Cytoskeleton

The Bacterial Actin-Like Cytoskeleton

The Bacterial Cytoskeleton

Treadmilling of a prokaryotic tubulin-like protein, TubZ, required for plasmid stability in Bacillus thuringiensis

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