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Journal of Bacteriology, April 2005, p. 2651-2661, Vol. 187, No. 8
0021-9193/05/$08.00+0     doi:10.1128/JB.187.8.2651-2661.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.

Protein Diversity Confers Specificity in Plasmid Segregation

Timothy J. G. Fothergill, Daniela Barillà, and Finbarr Hayes*

Faculty of Life Sciences, University of Manchester, Manchester, England

Received 4 October 2004/ Accepted 10 January 2005

The ParG segregation protein (8.6 kDa) of multidrug resistance plasmid TP228 is a homodimeric DNA-binding factor. The ParG dimer consists of intertwined C-terminal domains that adopt a ribbon-helix-helix architecture and a pair of flexible, unstructured N-terminal tails. A variety of plasmids possess partition loci with similar organizations to that of TP228, but instead of ParG homologs, these plasmids specify a diversity of unrelated, but similarly sized, partition proteins. These include the proteobacterial pTAR, pVT745, and pB171 plasmids. The ParG analogs of these plasmids were characterized in parallel with the ParG homolog encoded by the pseudomonal plasmid pVS1. Like ParG, the four proteins are dimeric. No heterodimerization was detectable in vivo among the proteins nor with the prototypical ParG protein, suggesting that monomer-monomer interactions are specific among the five proteins. Nevertheless, as with ParG, the ParG analogs all possess significant amounts of unordered amino acid residues, potentially highlighting a common structural link among the proteins. Furthermore, the ParG analogs bind specifically to the DNA regions located upstream of their homologous parF-like genes. These nucleoprotein interactions are largely restricted to cognate protein-DNA pairs. The results reveal that the partition complexes of these and related plasmids have recruited disparate DNA-binding factors that provide a layer of specificity to the macromolecular interactions that mediate plasmid segregation.

* Corresponding author. Mailing address: Faculty of Life Sciences, University of Manchester, Jackson's Mill, P.O. Box 88, Sackville St., Manchester M60 1QD, England. Phone: 44 161 3068934. Fax: 44 161 2360409. E-mail: finbarr.hayes{at}manchester.ac.uk.

Journal of Bacteriology, April 2005, p. 2651-2661, Vol. 187, No. 8
0021-9193/05/$08.00+0     doi:10.1128/JB.187.8.2651-2661.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Barilla, D., Carmelo, E., Hayes, F. (2007). The tail of the ParG DNA segregation protein remodels ParF polymers and enhances ATP hydrolysis via an arginine finger-like motif. Proc. Natl. Acad. Sci. USA 104: 1811-1816 [Abstract] [Full Text]  
  • Ringgaard, S., Ebersbach, G., Borch, J., Gerdes, K. (2007). Regulatory Cross-talk in the Double par Locus of Plasmid pB171. J. Biol. Chem. 282: 3134-3145 [Abstract] [Full Text]  
  • Yin, P., Li, T.-Y., Xie, M.-H., Jiang, L., Zhang, Y. (2006). A Type Ib ParB Protein Involved in Plasmid Partitioning in a Gram-Positive Bacterium. J. Bacteriol. 188: 8103-8108 [Abstract] [Full Text]  
  • Carmelo, E., Barilla, D., Golovanov, A. P., Lian, L.-Y., Derome, A., Hayes, F. (2005). The Unstructured N-terminal Tail of ParG Modulates Assembly of a Quaternary Nucleoprotein Complex in Transcription Repression. J. Biol. Chem. 280: 28683-28691 [Abstract] [Full Text]  


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