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Gene Review

sopA  -  plasmid-partitioning protein SopA

Escherichia coli

 
 
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Disease relevance of sopA

  • The F plasmid in Escherichia coli has its own partition mechanism controlled by the sopA and sopB genes, and by the cis-acting sopC region [1].
  • We report here that the Salmonella effector, SopA, interacts with host HsRMA1, a ubiquitin E3 ligase with a previously unknown function [2].
  • SopA, the outer membrane protease responsible for polar localization of IcsA in Shigella flexneri [3].
  • A locus close to one end of the linear N15 prophage closely resembles the sop operon which governs partition of the F plasmid; the promoter region contains similar operator sites, and the two putative gene products have extensive amino acid identity with the SopA and -B proteins of F [4].
 

High impact information on sopA

  • When SopA is polymerized in vitro in the presence of SopB and sopC-containing DNA, SopA filaments emanate from the plasmid DNA in radial asters [5].
  • Our data suggest that efficient bacterial escape into the cytosol of epithelial cells requires HsRMA1-mediated SopA ubiquitination and contributes to Salmonella-induced enteropathogenicity [2].
  • SopA binds to four repeated sequences (CTTTGC) located in the promoter-operator region of the sopAB operon [6].
  • In this study, we purified independently SopA and SopB proteins, analyzed the in vitro DNA-binding activity of these proteins by the gel retardation assay, and determined the precise binding sites of DNA by the footprinting method [6].
  • Disruption of the F plasmid partition complex in vivo by partition protein SopA [7].
 

Biological context of sopA

  • Here we demonstrate that the F-plasmid-partitioning protein SopA polymerizes into filaments in an ATP-dependent manner in vitro, and that the filaments elongate at a rate that is similar to that of plasmid separation in vivo [5].
  • Deletion analyses revealed that the mini-F segment responsible for the inhibition of both processes was the promoter region of the sopA gene which had been cloned into a site upstream of the bla gene on pBR322 in such an orientation as to cause overexpression of bla [8].
  • The sopA, B, C genes of the F plasmid play an essential role in plasmid partitioning during cell division in Escherichia coli [9].
  • The results are interpreted in terms of a regulatory role for SopA in the oligomerization of SopB dimers bound to the centromere [7].
  • The construction and phenotypic characterization of a sopA mutant demonstrated that SopA is required for exclusive polar localization of IcsA on the bacterial surface and proper expression of the motility phenotype in infected cells [3].
 

Associations of sopA with chemical compounds

  • Maintenance of the unipolar distribution of IcsA depends on both the S. flexneri outer membrane protease IcsP (SopA) and the structure of the lipopolysaccharide (LPS) in the outer membrane [10].
 

Analytical, diagnostic and therapeutic context of sopA

References

  1. Structure and function of the F plasmid genes essential for partitioning. Mori, H., Kondo, A., Ohshima, A., Ogura, T., Hiraga, S. J. Mol. Biol. (1986) [Pubmed]
  2. Recognition and ubiquitination of Salmonella type III effector SopA by a ubiquitin E3 ligase, HsRMA1. Zhang, Y., Higashide, W., Dai, S., Sherman, D.M., Zhou, D. J. Biol. Chem. (2005) [Pubmed]
  3. SopA, the outer membrane protease responsible for polar localization of IcsA in Shigella flexneri. Egile, C., d'Hauteville, H., Parsot, C., Sansonetti, P.J. Mol. Microbiol. (1997) [Pubmed]
  4. Partition of the linear plasmid N15: interactions of N15 partition functions with the sop locus of the F plasmid. Ravin, N., Lane, D. J. Bacteriol. (1999) [Pubmed]
  5. Bacterial DNA segregation by dynamic SopA polymers. Lim, G.E., Derman, A.I., Pogliano, J. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  6. Purification and characterization of SopA and SopB proteins essential for F plasmid partitioning. Mori, H., Mori, Y., Ichinose, C., Niki, H., Ogura, T., Kato, A., Hiraga, S. J. Biol. Chem. (1989) [Pubmed]
  7. Disruption of the F plasmid partition complex in vivo by partition protein SopA. Lemonnier, M., Bouet, J.Y., Libante, V., Lane, D. Mol. Microbiol. (2000) [Pubmed]
  8. Inhibition of cell growth and stable DNA replication by overexpression of the bla gene of plasmid pBR322 in Escherichia coli. Katayama, T., Nagata, T. Mol. Gen. Genet. (1990) [Pubmed]
  9. ATPase activity of SopA, a protein essential for active partitioning of F plasmid. Watanabe, E., Wachi, M., Yamasaki, M., Nagai, K. Mol. Gen. Genet. (1992) [Pubmed]
  10. Actin-based motility is sufficient for bacterial membrane protrusion formation and host cell uptake. Monack, D.M., Theriot, J.A. Cell. Microbiol. (2001) [Pubmed]
  11. Subcellular positioning of F plasmid mediated by dynamic localization of SopA and SopB. Adachi, S., Hori, K., Hiraga, S. J. Mol. Biol. (2006) [Pubmed]
 
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