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

• We have analyzed by immunofluorescence microscopy the subcellular localization of SopA and SopB [11].

References