Patchiness of murein insertion into the sidewall of Escherichia coli

Microbiology ◽  
2003 ◽  
Vol 149 (7) ◽  
pp. 1753-1761 ◽  
Author(s):  
Miguel A. De Pedro ◽  
Heinz Schwarz ◽  
Arthur L. Koch
Keyword(s):  
Escherichia Coli ◽  
Cell Division ◽  
Gram Negative ◽  
New Material ◽  
Wall Growth ◽  
Kinetics Of ◽  
Made In

This paper extends, with computer techniques, the authors' previous work on the kinetics of pole wall and sidewall synthesis in Escherichia coli. These findings extend the conclusion that the nascent poles are made of entirely new material and that no new material is inserted into old poles. This requires re-evaluation of ideas in the literature about wall growth and cell division. Mechanisms of various types have been suggested for the growth of Gram-negative rod-shaped bacteria and these will also require major re-evaluation because of the finding, reported here, that the sidewall is made in several modes: patches of new murein, bands of new material largely going circumferentially around the cell, and areas of the sidewall that are enlarged by an intimate and regular admixture of new with the old muropeptides.

scholarly journals MexAB-OprM Efflux Pump Interaction with the Peptidoglycan of Escherichia coli and Pseudomonas aeruginosa

2021 ◽  
Vol 22 (10) ◽  
pp. 5328
Author(s):  
Miao Ma ◽  
Margaux Lustig ◽  
Michèle Salem ◽  
Dominique Mengin-Lecreulx ◽  
Gilles Phan ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Pseudomonas Aeruginosa ◽  
Cell Division ◽  
Membrane Proteins ◽  
Outer Membrane ◽  
Efflux Pump ◽  
Gram Negative Bacteria ◽  
Gram Negative ◽  
Active Efflux

One of the major families of membrane proteins found in prokaryote genome corresponds to the transporters. Among them, the resistance-nodulation-cell division (RND) transporters are highly studied, as being responsible for one of the most problematic mechanisms used by bacteria to resist to antibiotics, i.e., the active efflux of drugs. In Gram-negative bacteria, these proteins are inserted in the inner membrane and form a tripartite assembly with an outer membrane factor and a periplasmic linker in order to cross the two membranes to expulse molecules outside of the cell. A lot of information has been collected to understand the functional mechanism of these pumps, especially with AcrAB-TolC from Escherichia coli, but one missing piece from all the suggested models is the role of peptidoglycan in the assembly. Here, by pull-down experiments with purified peptidoglycans, we precise the MexAB-OprM interaction with the peptidoglycan from Escherichia coli and Pseudomonas aeruginosa, highlighting a role of the peptidoglycan in stabilizing the MexA-OprM complex and also differences between the two Gram-negative bacteria peptidoglycans.

scholarly journals FtsZ Directs a Second Mode of Peptidoglycan Synthesis in Escherichia coli

2007 ◽  
Vol 189 (15) ◽  
pp. 5692-5704 ◽  
Author(s):  
Archana Varma ◽  
Miguel A. de Pedro ◽  
Kevin D. Young
Keyword(s):  
Escherichia Coli ◽  
Cell Formation ◽  
Lateral Wall ◽  
Penicillin Binding Protein ◽  
E Coli ◽  
Protein Mutants ◽  
Central Regions ◽  
New Material ◽  
Side Walls ◽  
Wall Growth

ABSTRACT Certain penicillin binding protein mutants of Escherichia coli grow with spirillum-like morphologies when the FtsZ protein is inhibited, suggesting that FtsZ might govern aspects of cell wall growth other than those strictly associated with septation. While investigating the mechanism of spiral cell formation, we discovered conditions for visualizing this second function of FtsZ. Normally, inhibiting the cytoskeleton protein MreB forces E. coli cells to grow as smoothly enlarging spheres from which the poles disappear, yielding coccoid or lemon-shaped forms. However, when FtsZ and MreB were inhibited simultaneously in a strain lacking PBP 5 and PBP 7, the resulting cells ballooned outward but retained conspicuous rod-shaped extensions at sites representing the original poles. This visual phenotype was paralleled by the biochemistry of sacculus growth. Muropeptides are usually inserted homogeneously into the lateral cell walls, but when FtsZ polymerization was inhibited, the incorporation of new material occurred mainly in the central regions of cells and was significantly lower in those portions of side walls abutting a pole. Thus, reduced precursor incorporation into side walls near the poles explained why these regions retained their rod-like morphology while the rest of the cell grew spherically. Also, inhibiting FtsZ increased the amount of pentapeptides in sacculi by about one-third. Finally, the MreB protein directed the helical or diagonal incorporation of new peptidoglycan into the wall, but the location of that incorporation depended on whether FtsZ was active. In sum, the results indicate that in addition to nucleating cell septation in E. coli, FtsZ can direct the insertion of new peptidoglycan into portions of the lateral wall.

scholarly journals Bacterial Metal Resistance: Coping with Copper without Cooperativity?

mBio ◽  
2021 ◽  
Author(s):  
Nicholas P. Greene ◽  
Vassilis Koronakis
Keyword(s):  
Escherichia Coli ◽  
Cell Division ◽  
Cell Envelope ◽  
Metal Resistance ◽  
Gram Negative Bacteria ◽  
Gram Negative ◽  
Content Type ◽  
E Coli ◽  
Rnd Transporter ◽  
Entire Cell

In Escherichia coli and other Gram-negative bacteria, tripartite efflux pumps (TEPs) span the entire cell envelope and serve to remove noxious molecules from the cell. CusBCA is a TEP responsible for copper and silver detoxification in E. coli powered by the resistance-nodulation-cell division (RND) transporter, CusA.

scholarly journals YtfB, an OapA Domain-Containing Protein, Is a New Cell Division Protein in Escherichia coli

2018 ◽  
Vol 200 (13) ◽  
Author(s):  
Matthew A. Jorgenson ◽  
Kevin D. Young
Keyword(s):  
Escherichia Coli ◽  
Cell Wall ◽  
Cell Division ◽  
Wall Structure ◽  
Bacterial Cell Division ◽  
Negative Bacterium ◽  
Gram Negative ◽  
Content Type ◽  
Cell Division Protein ◽  
Inner Membrane Protein

ABSTRACT While screening the Pfam database for novel peptidoglycan (PG) binding modules, we identified the OapA domain, which is annotated as a LysM-like domain. LysM domains bind PG and mediate localization to the septal ring. In the Gram-negative bacterium Escherichia coli , an OapA domain is present in YtfB, an inner membrane protein of unknown function but whose overproduction causes cells to filament. Together, these observations suggested that YtfB directly affects cell division, most likely through its OapA domain. Here, we show that YtfB accumulates at the septal ring and that its action requires the division-initiating protein FtsZ and, to a lesser extent, ZipA, an early recruit to the septalsome. While the loss of YtfB had no discernible impact, a mutant lacking both YtfB and DedD (a known cell division protein) grew as filamentous cells. The YtfB OapA domain by itself also localized to sites of division, and this localization was enhanced by the presence of denuded PGs. Finally, the OapA domain bound PG, though binding did not depend on the formation of denuded glycans. Collectively, our findings demonstrate that YtfB is a cell division protein whose function is related to cell wall hydrolases. IMPORTANCE All living cells must divide in order to thrive. In bacteria, this involves the coordinated activities of a large number of proteins that work in concert to constrict the cell. Knowing which proteins contribute to this process and how they function is fundamental. Here, we identify a new member of the cell division apparatus in the Gram-negative bacterium Escherichia coli whose function is related to the generation of a transient cell wall structure. These findings deepen our understanding of bacterial cell division.

scholarly journals Kinetics of large-scale chromosomal movement during asymmetric cell division in Escherichia coli

PLoS Genetics ◽  
2017 ◽  
Vol 13 (2) ◽  
pp. e1006638 ◽  
Author(s):  
Jaana Männik ◽  
Matthew W. Bailey ◽  
Jordan C. O’Neill ◽  
Jaan Männik
Keyword(s):  
Escherichia Coli ◽  
Cell Division ◽  
Large Scale ◽  
Asymmetric Cell Division ◽  
Kinetics Of

Analysis of cell division in rapidly growing synchronous cultures of Escherichia coli recovering from an inhibition of deoxyribonucleic acid synthesis

1973 ◽  
Vol 19 (9) ◽  
pp. 1111-1114 ◽  
Author(s):  
George G. Khachatourians ◽  
Lorraine M. McGrath
Keyword(s):  
Escherichia Coli ◽  
Cell Division ◽  
Deoxyribonucleic Acid ◽  
Acid Synthesis ◽  
Short Pulses ◽  
Synchronous Cultures ◽  
Deoxyribonucleic Acid Synthesis ◽  
Casamino Acids ◽  
Inhibition Of Dna Synthesis ◽  
Kinetics Of

Kinetics of cell division in cultures of Escherichia coli grown in casamino acids – glucose and recovering from short pulses of inhibition of DNA synthesis by nalidixic acid clearly demonstrates that preexisting cycles of chromosome replication continue to their ends.

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