Role of Leucine Zipper Motifs in Association of the Escherichia coli Cell Division Proteins FtsL and FtsB

Institut Pasteur, CNRS URA 2185, Unité de Biochimie des Interactions Macromoléculaires, Département de Biologie Structurale et Chimie, 28 rue du Dr Roux, 75724 Paris Cedex 15, France.
Journal of bacteriology (Impact Factor: 2.81). 07/2011; 193(18):4988-92. DOI: 10.1128/JB.00324-11
Source: PubMed


FtsL and FtsB are two inner-membrane proteins that are essential constituents of the cell division apparatus of Escherichia coli. In this study, we demonstrate that the leucine zipper-like (LZ) motifs, located in the periplasmic domain of FtsL and FtsB,
are required for an optimal interaction between these two essential proteins.

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    • "Consequently, PPI of two membrane proteins fused to adenylate cyclase fragments results in fermentation of lactose or maltose which can easily be detected on either indicator (MacConkey maltose or X-Gal plates) or selection media (minimal media supplemented with either lactose or maltose as carbon source) (Karimova, Dautin, and Ladant 2005). In addition, BACTH allows quantification of the PPI by measuring the activity of the lactose cleaving β-galactosidase (Robichon et al. 2011). Fig. 2. The bacterial adenylate cyclase two-hybrid assay (BACTH). "

    Full-text · Chapter · Mar 2012
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    ABSTRACT: The bacterial two-hybrid system based on the reconstitution of adenylate cyclase in Escherichia coli (BACTH) was described 14years ago (Karimova, Pidoux, Ullmann, and Ladant, 1998, PNAS, 95:5752). For microbiologists, it is a practical and powerful alternative to the use of the widely spread yeast two-hybrid technology for testing protein-protein interactions. In this review, we aim at giving the reader clear and most importantly simple instructions that should break any reticence to try the technique. Yet, we also add recommendations in the use of the system, related to its specificities. Finally, we expose the advantages and disadvantages of the technique, and review its diverse applications in the literature, which should help in deciding if it is the appropriate method to choose for the case at hand.
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    ABSTRACT: In Escherichia coli, cell division is performed by a multimolecular machinery called the divisome, made of 10 essential proteins and more than 20 accessory proteins. Through a bacterial two-hybrid library screen, we identified the E. coli β-lactam resistance protein Blr, a short membrane polypeptide of 41 residues, as an interacting partner of the essential cell division protein FtsL. In addition to FtsL, Blr was found to associate with several other divisomal proteins, including FtsI, FtsK, FtsN, FtsQ, FtsW, and YmgF. Using fluorescently tagged Blr, we showed that this peptide localizes to the division septum and that its colocalization requires the presence of the late division protein FtsN. Although Blr is not essential, previous studies have shown that the inactivation of the blr gene increased the sensitivity of bacteria to β-lactam antibiotics or their resistance to cell envelope stress. Here, we found that Blr, when overproduced, restores the viability of E. coli ftsQ1(Ts) cells, carrying a thermosensitive allele of the ftsQ gene, during growth under low-osmotic-strength conditions (e.g., in synthetic media or in Luria-Bertani broth without NaCl). In contrast, the inactivation of blr increases the osmosensitivity of ftsQ1(Ts) cells, and blr ftsQ1 double mutants exhibit filamentous growth in LB broth even at a moderate salt concentration (0.5% NaCl) compared to parental ftsQ1(Ts) cells. Altogether, our results suggest that the small membrane polypeptide Blr is a novel component of the E. coli cell division apparatus involved in the stabilization of the divisome under certain stress conditions.
    Preview · Article · Aug 2012 · Journal of bacteriology
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