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Article
Subject Categories: Cell Cycle | Microbiology & Pathogens
The EMBO Journal (2005) 24, 1453–1464, doi:10.1038/sj.emboj.7600619
Published online 10 March 2005
Bacterial DNA segregation dynamics mediated by the polymerizing protein ParF
Daniela Barillà1, Mark F Rosenberg1, Ulf Nobbmann2 and Finbarr Hayes1
1 Faculty of Life Sciences, University of Manchester, Manchester, UK
2 Malvern Instruments Ltd, Malvern, Worcestershire, UK

To whom correspondence should be addressed
Finbarr Hayes, Faculty of Life Sciences, The University of Manchester, PO Box 88, Sackville Street, Manchester M60 1QD, UK. Tel.: +44 161 200 8934; Fax: +44 161 236 0409; E-mail: finbarr.hayes@manchester.ac.uk

Received 30 August 2004; Accepted 15 February 2005; Published online 10 March 2005.
Abstract
Prokaryotic DNA segregation most commonly involves members of the Walker-type ParA superfamily. Here we show that the ParF partition protein specified by the TP228 plasmid is a ParA ATPase that assembles into extensive filaments in vitro. Polymerization is potentiated by ATP binding and does not require nucleotide hydrolysis. Analysis of mutations in conserved residues of the Walker A motif established a functional coupling between filament dynamics and DNA partitioning. The partner partition protein ParG plays two separable roles in the ParF polymerization process. ParF is unrelated to prokaryotic polymerizing proteins of the actin or tubulin families, but is a homologue of the MinD cell division protein, which also assembles into filaments. The ultrastructures of the ParF and MinD polymers are remarkably similar. This points to an evolutionary parallel between DNA segregation and cytokinesis in prokaryotic cells, and reveals a potential molecular mechanism for plasmid and chromosome segregation mediated by the ubiquitous ParA-type proteins.
Keywords: DNA segregation, ParA, ParF, plasmid, polymerization
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