scholarly journals The mecillinam resistome reveals a role for peptidoglycan endopeptidases in stimulating cell wall synthesis in Escherichia coli

PLoS Genetics ◽  
2017 ◽  
Vol 13 (7) ◽  
pp. e1006934 ◽  
Author(s):  
Ghee Chuan Lai ◽  
Hongbaek Cho ◽  
Thomas G. Bernhardt
Keyword(s):  
Escherichia Coli ◽  
Cell Wall ◽  
Cell Wall Synthesis

scholarly journals Interactions between Penicillin-Binding Proteins (PBPs) and Two Novel Classes of PBP Inhibitors, Arylalkylidene Rhodanines and Arylalkylidene Iminothiazolidin-4-ones

2004 ◽  
Vol 48 (3) ◽  
pp. 961-969 ◽  
Author(s):  
Astrid Zervosen ◽  
Wei-Ping Lu ◽  
Zhouliang Chen ◽  
Ronald E. White ◽  
Thomas P. Demuth ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Cell Wall ◽  
Cell Wall Synthesis ◽  
Bacterial Strains ◽  
Gram Negative ◽  
Penicillin Binding Proteins ◽  
E Coli ◽  
Peptidoglycan Biosynthesis ◽  
Vancomycin Resistant ◽  
Inhibitory Activities

ABSTRACT Several non-β-lactam compounds were active against various gram-positive and gram-negative bacterial strains. The MICs of arylalkylidene rhodanines and arylalkylidene iminothiazolidin-4-ones were lower than those of ampicillin and cefotaxime for methicillin-resistant Staphylococcus aureus MI339 and vancomycin-resistant Enterococcus faecium EF12. Several compounds were found to inhibit the cell wall synthesis of S. aureus and the last two steps of peptidoglycan biosynthesis catalyzed by ether-treated cells of Escherichia coli or cell wall membrane preparations of Bacillus megaterium. The effects of the arylalkylidene rhodanines and arylalkylidene iminothiazolidin-4-one derivatives on E. coli PBP 3 and PBP 5, Streptococcus pneumoniae PBP 2xS (PBP 2x from a penicillin-sensitive strain) and PBP 2xR (PBP 2x from a penicillin-resistant strain), low-affinity PBP 2a of S. aureus, and the Actinomadura sp. strain R39 and Streptomyces sp. strain R61 dd-peptidases were studied. Some of the compounds exhibited inhibitory activities in the 10 to 100 μM concentration range. The inhibition of PBP 2xS by several of them appeared to be noncompetitive. The dissociation constant for the best inhibitor (Ki = 10 μM) was not influenced by the presence of the substrate.

Bactericidal action of peptide antibiotic AS-48 against Escherichia coli K-12

1989 ◽  
Vol 35 (2) ◽  
pp. 318-321 ◽  
Author(s):  
A. Gálvez ◽  
E. Valdivia ◽  
M. Martínez ◽  
M. Maqueda
Keyword(s):  
Escherichia Coli ◽  
Cell Wall ◽  
Cell Growth ◽  
Mode Of Action ◽  
Cytoplasmic Membrane ◽  
Peptide Antibiotic ◽  
Biosynthetic Pathways ◽  
Bactericidal Action ◽  
Cell Wall Synthesis ◽  
K 12

Peptide antibiotic AS-48 exerts a bactericidal mode of action on exponential cultures of Escherichia coli K-12 through a multi-hit kinetics interaction. AS-48 causes a parallel and gradual cessation of all biosynthetic pathways monitored (protein, RNA, DNA, and cell wall synthesis), the rate of incorporation of labeled precursors, the rate of O2 consumption, and cell growth. These effects have been attributed to alterations of cytoplasmic membrane functions.Key words: Escherichia coli, peptide antibiotic, bactericide.

scholarly journals FtsN activates septal cell wall synthesis by forming a processive complex with the septum-specific peptidoglycan synthase in E. coli

2021 ◽  
Author(s):  
Zhixin Lyu ◽  
Atsushi Yahashiri ◽  
Xinxing Yang ◽  
Joshua W McCausland ◽  
Gabriela M Kaus ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Cell Wall ◽  
Single Molecule ◽  
Spatial Organization ◽  
Genetic Manipulation ◽  
Cell Wall Synthesis ◽  
Single Population ◽  
E Coli ◽  
Ftsz Ring ◽  
Synthesis Activity

The FtsN protein of Escherichia coli and other proteobacteria is an essential and highly conserved bitopic membrane protein that triggers the inward synthesis of septal peptidoglycan (sPG) during cell division. Previous work has shown that the activation of sPG synthesis by FtsN involves a series of interactions of FtsN with other divisome proteins and the cell wall. Precisely how FtsN achieves this role is unclear, but a recent study has shown that FtsN promotes the relocation of the essential sPG synthase FtsWI from an FtsZ-associated track (where FtsWI is inactive) to an sPG-track (where FtsWI engages in sPG synthesis). Whether FtsN works by displacing FtsWI from the Z-track or capturing/retaining FtsWI on the sPG-track is not known. Here we use single-molecule imaging and genetic manipulation to investigate the organization and dynamics of FtsN at the septum and how they are coupled to sPG synthesis activity. We found that FtsN exhibits a spatial organization and dynamics distinct from those of the FtsZ-ring. Single FtsN molecules move processively as a single population with a speed of ~ 9 nm s-1, similar to the speed of active FtsWI molecules on the sPG-track, but significantly different from the ~ 30 nm s-1 speed of inactive FtsWI molecules on the FtsZ-track. Furthermore, the processive movement of FtsN is independent of FtsZ's treadmilling dynamics but driven exclusively by active sPG synthesis. Importantly, only the essential domain of FtsN, a three-helix bundle in the periplasm, is required to maintain the processive complex containing both FtsWI and FtsN on the sPG-track. We conclude that FtsN activates sPG synthesis by forming a processive synthesis complex with FtsWI exclusively on the sPG-track. These findings favor a model in which FtsN captures or retains FtsWI on the sPG-track rather than one in which FtsN actively displaces FtsWI from the Z-track.

scholarly journals GTPase activity-coupled treadmilling of the bacterial tubulin FtsZ organizes septal cell-wall synthesis

2016 ◽  
Author(s):  
Xinxing Yang ◽  
Zhixin Lyu ◽  
Amanda Miguel ◽  
Ryan McQuillen ◽  
Kerwyn Casey Huang ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Cell Wall ◽  
Spatial Distribution ◽  
Molecular Composition ◽  
Central Component ◽  
Gtpase Activity ◽  
Cell Wall Synthesis ◽  
Gtp Hydrolysis

AbstractThe bacterial tubulin FtsZ is the central component of the division machinery, coordinating an ensemble of proteins involved in septal cell-wall synthesis to ensure successful constriction. How cells achieve this coordination is unknown. We used a combination of imaging, genetic and biochemical approaches to demonstrate that in Escherichia coli cells FtsZ exhibits dynamic treadmilling predominantly determined by its GTPase activity, and that the treadmilling dynamics directs processive movement of the septal cell-wall synthesis machinery. In FtsZ mutants with severely reduced treadmilling, the spatial distribution of septal synthesis and the molecular composition and ultrastructure of the septal cell wall are substantially altered. Thus, the treadmilling of FtsZ provides a novel and robust mechanism for achieving uniform septal cell-wall synthesis to enable correct new pole morphology.One-sentence summaryThe bacterial tubulin FtsZ uses GTP hydrolysis to power treadmilling, driving processive synthesis of the septal cell wall.

scholarly journals Binding of D-methionine to peptidoglycan in the presence of inhibitors of cell wall synthesis in Escherichia coli.

1985 ◽  
Vol 49 (8) ◽  
pp. 2489-2490 ◽  
Author(s):  
Tsutomu TSURUOKA ◽  
Atsushi TAMURA ◽  
Yuji MATSUHASHI ◽  
Tamako TAKEI ◽  
Shigeharu INOUYE ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Cell Wall ◽  
Cell Wall Synthesis

scholarly journals FtsEX acts on FtsA to regulate divisome assembly and activity

2016 ◽  
Vol 113 (34) ◽  
pp. E5052-E5061 ◽  
Author(s):  
Shishen Du ◽  
Sebastien Pichoff ◽  
Joe Lutkenhaus
Keyword(s):  
Escherichia Coli ◽  
Cell Wall ◽  
Cell Division ◽  
Atpase Activity ◽  
Critical Role ◽  
Bacterial Cell Division ◽  
Cell Wall Synthesis ◽  
Atp Binding Cassette Transporter ◽  
Inactive Form ◽  
Cell Wall Hydrolysis

Bacterial cell division is driven by the divisome, a ring-shaped protein complex organized by the bacterial tubulin homolog FtsZ. Although most of the division proteins inEscherichia colihave been identified, how they assemble into the divisome and synthesize the septum remains poorly understood. Recent studies suggest that the bacterial actin homolog FtsA plays a critical role in divisome assembly and acts synergistically with the FtsQLB complex to regulate the activity of the divisome. FtsEX, an ATP-binding cassette transporter-like complex, is also necessary for divisome assembly and inhibits division when its ATPase activity is inactivated. However, its role in division is not clear. Here, we find that FtsEX acts on FtsA to regulate both divisome assembly and activity. FtsX interacts with FtsA and this interaction is required for divisome assembly and inhibition of divisome function by ATPase mutants of FtsEX. Our results suggest that FtsEX antagonizes FtsA polymerization to promote divisome assembly and the ATPase mutants of FtsEX block divisome activity by locking FtsA in the inactive form or preventing FtsA from communicating with other divisome proteins. Because FtsEX is known to govern cell wall hydrolysis at the septum, our findings indicate that FtsEX acts on FtsA to promote divisome assembly and to coordinate cell wall synthesis and hydrolysis at the septum. Furthermore, our study provides evidence that FtsA mutants impaired for self-interaction are favored for division, and FtsW plays a critical role in divisome activation in addition to the FtsQLB complex.

scholarly journals Regeneration of Escherichia coli Giant Protoplasts to Their Original Form

Life ◽  
2019 ◽  
Vol 9 (1) ◽  
pp. 24 ◽  
Author(s):  
Kazuhito V. Tabata ◽  
Takao Sogo ◽  
Yoshiki Moriizumi ◽  
Hiroyuki Noji
Keyword(s):  
Escherichia Coli ◽  
Cell Wall ◽  
Bacillus Subtilis ◽  
Colony Formation ◽  
Cell Walls ◽  
Microscopic Investigation ◽  
Original Form ◽  
Cell Wall Synthesis ◽  
E Coli ◽  
The Relationship

The spheroplasts and protoplasts of cell wall-deficient (CWD) bacteria are able to revert to their original cellular morphologies through the regeneration of their cell walls. However, whether this is true for giant protoplasts (GPs), which can be as large as 10 μm in diameter, is unknown. GPs can be prepared from various bacteria, including Escherichia coli and Bacillus subtilis, and also from fungi, through culture in the presence of inhibitors for cell wall synthesis or mitosis. In this report, we prepared GPs from E. coli and showed that they can return to rod-shaped bacterium, and that they are capable of colony formation. Microscopic investigation revealed that the regeneration process took place through a variety of morphological pathways. We also report the relationship between GP division and GP volume. Finally, we show that FtsZ is crucial for GP division. These results indicate that E. coli is a highly robust organism that can regenerate its original form from an irregular state, such as GP.

scholarly journals Sublethal Concentrations of Ciprofloxacin Induce Bacteriocin Synthesis in Escherichia coli

2005 ◽  
Vol 49 (7) ◽  
pp. 3087-3090 ◽  
Author(s):  
Borut Jerman ◽  
Matej Butala ◽  
Darja Žgur-Bertok
Keyword(s):  
Escherichia Coli ◽  
Cell Wall ◽  
Dna Replication ◽  
Sos Response ◽  
Dependent Manner ◽  
Cell Wall Synthesis ◽  
Narrow Spectrum ◽  
Sublethal Concentrations

ABSTRACT Antibiotics that interfere with DNA replication, as well as cell wall synthesis, induce the SOS response. In this report, we show that ciprofloxacin induces synthesis of colicins, narrow-spectrum antibiotics frequently produced by Escherichia coli strains, in an SOS-dependent manner.

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