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

Robichon, Carine; Karimova, Gouzel; Beckwith, Jon; Ladant, Daniel

doi:10.1128/jb.00324-11

Cited by 39 publications

(48 citation statements)

References 30 publications

(56 reference statements)

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“…Consistently, studies have shown interdependencies of FtsQ, FtsB, and FtsL for stability and localization at the divisome in different species (15)(16)(17)(18)(19). FtsB and FtsL are small (103 and 121 residues, respectively) bitopic inner membrane proteins with a predicted mainly ␣-helical structure (3,11,18).…”

supporting

confidence: 52%

“…Like FtsQ, they have been suggested to fulfill a scaffolding function in divisome assembly (18). In the absence of FtsQ, the proteins FtsB and FtsL form a subcomplex, presumably through interactions between their TMs and membrane-proximal periplasmic regions that contain a leucine zipper motif (19). The FtsBL subcomplex requires FtsQ for localization to the midcell (20), but it can independently recruit downstream division proteins when targeted prematurely to the divisome (17).…”

mentioning

confidence: 99%

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The Soluble Periplasmic Domains of Escherichia coli Cell Division Proteins FtsQ/FtsB/FtsL Form a Trimeric Complex with Submicromolar Affinity

Glas

Saparoea

McLaughlin

et al. 2015

Journal of Biological Chemistry

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supporting

confidence: 52%

mentioning

confidence: 99%

The Soluble Periplasmic Domains of Escherichia coli Cell Division Proteins FtsQ/FtsB/FtsL Form a Trimeric Complex with Submicromolar Affinity

Glas

Saparoea

McLaughlin

et al. 2015

Journal of Biological Chemistry

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“…To generate polyclonal anti-PbpX, anti-PbpY, and anti-PbpC antibodies, rabbits were immunized with mixtures of the PbpX-derived peptides AEAPAGEPPPADQLPY and DYNDSQFDRATT ARRQ, the PbpY-derived peptides CAAQPGKPTQKPDPLS and MPDA GELQDYRPPTAT, or the PbpC-derived peptides CVAPAPGQPPPD NLPY and LPPYKFDDGKSPGEPC (Eurogentec). Immunoblot analysis was performed as described previously (28), using anti-CtrA (29) (1: 10,000), anti-PbpX (1:2,500), anti-PbpY (1:2,500), anti-PbpC (1:10,000), or anti-CyaA (T25) (30) antiserum or a monoclonal anti-green fluorescent protein (anti-GFP) (Sigma-Aldrich) (1:10,000) or anti-CyaA (T18) (3D1; Santa Cruz Biotechnology) (1:100) antibody. Immunocomplexes were visualized using the Western Lightning chemiluminescence reagent (PerkinElmer) and Hyperfilm ECL (GE Healthcare) autoradiography films.…”

Section: Methodsmentioning

confidence: 99%

Function and Localization Dynamics of Bifunctional Penicillin-Binding Proteins in Caulobacter crescentus

et al. 2014

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The peptidoglycan cell wall of bacteria is a complex macromolecule composed of glycan strands that are cross-linked by short peptide bridges. Its biosynthesis involves a conserved group of enzymes, the bifunctional penicillin-binding proteins (bPBPs), which contain both a transglycosylase and a transpeptidase domain, thus being able to elongate the glycan strands and, at the same time, generate the peptide cross-links. The stalked model bacterium Caulobacter crescentus possesses five bPBP paralogs, named Pbp1A, PbpC, PbpX, PbpY, and PbpZ, whose function is still incompletely understood. In this study, we show that any of these proteins except for PbpZ is sufficient for growth and normal morphogenesis when expressed at native or elevated levels, whereas inactivation of all five paralogs is lethal. Growth analyses indicate a central role of PbpX in the resistance of C. crescentus against the noncanonical amino acid D-alanine. Moreover, we show that PbpX and PbpY localize to the cell division site. Their recruitment to the divisome is dependent on the essential cell division protein FtsN and likely involves interactions with FtsL and the putative peptidoglycan hydrolase DipM. The same interaction pattern is observed for Pbp1A and PbpC, although these proteins do not accumulate at midcell. Our findings demonstrate that the bPBPs of C. crescentus are, to a large extent, redundant and have retained the ability to interact with the peptidoglycan biosynthetic machineries responsible for cell elongation, cytokinesis, and stalk growth. Nevertheless, they may preferentially act in specific peptidoglycan biosynthetic complexes, thereby facilitating the independent regulation of distinct growth processes.

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“…For BACTH complementation assays, Blr variants were genetically fused to T25 or T18 fragments of the catalytic domain of Bordetella pertussis adenylate cyclase and coexpressed with various E. coli divisomal proteins in DHM1 cells. After transformation, cells harboring a pair of the appropriate plasmids were plated onto LB agar containing X-Gal and IPTG plus antibiotics and incubated at 30°C for 24 to 36 h. The efficiency of the interaction between two tested hybrid proteins was quantified by measuring the ␤-galactosidase (␤-Gal) activity in liquid cultures in a 96-well format based on an assay described previously (26,46). For each set of transformations, the ␤-Gal assay was performed on eight cultures that were grown overnight at 30°C in 300 l LB broth in the presence of 0.5 mM IPTG and the appropriate antibiotics in a 96-well microtiter plate (2.2-ml 96-well storage plate; Thermo Fisher Scientific).…”

Section: Methodsmentioning

confidence: 99%

The β-Lactam Resistance Protein Blr, a Small Membrane Polypeptide, Is a Component of the Escherichia coli Cell Division Machinery

2012

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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 ␤-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 ␤-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.

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

Cited by 39 publications

References 30 publications

The Soluble Periplasmic Domains of Escherichia coli Cell Division Proteins FtsQ/FtsB/FtsL Form a Trimeric Complex with Submicromolar Affinity

The Soluble Periplasmic Domains of Escherichia coli Cell Division Proteins FtsQ/FtsB/FtsL Form a Trimeric Complex with Submicromolar Affinity

Function and Localization Dynamics of Bifunctional Penicillin-Binding Proteins in Caulobacter crescentus

The β-Lactam Resistance Protein Blr, a Small Membrane Polypeptide, Is a Component of the Escherichia coli Cell Division Machinery

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