scholarly journals RodZ: a key-player in cell elongation and cell division in Escherichia coli

2019 ◽  
Vol 5 (4) ◽  
pp. 358-367 ◽  
Author(s):  
Risa Ago ◽  
◽  
Daisuke Shiomi
Keyword(s):  
Escherichia Coli ◽  
Cell Division ◽  
Cell Elongation

The cytological effects of myxin on Escherichia coli

1969 ◽  
Vol 15 (7) ◽  
pp. 707-711 ◽  
Author(s):  
I. L. Stevenson
Keyword(s):  
Escherichia Coli ◽  
Plasma Membrane ◽  
Cell Division ◽  
Cell Surface ◽  
Microscopic Examination ◽  
Cell Elongation ◽  
Nuclear Bodies ◽  
Abnormal Development ◽  
Macromolecular Synthesis ◽  
Apparent Effect

When actively growing cells of Escherichia coli 15T− were treated with the new antibiotic myxin, the effects produced by the antibiotic varied, depending on the concentration. With a concentration of 1 μg/ml, the action was bacteriostatic for the first 60 min exposure. Cell division was inhibited but there was no apparent effect on macromolecular synthesis as evidenced by the formation of filamentous cells. At higher concentrations (3 and 5 μg/ml), myxin was bactericidal although some cell elongation occurred at the 3 μg/ml level. Microscopic examination of cells treated with 3 and 5 μg/ml for 30–45 min indicated the presence of vacuolated areas which thin section studies revealed as intracellular ramifications of the plasma membrane. Protoplasts of cells grown in the presence of 5 μg/ml myxin were enlarged or rapidly lysed even after as little as 15 min exposure. Myxin has no effect on the cell surface of control protoplasts. No abnormal development of the plasma membrane was noted in the elongated cells formed in the presence of 1 μg/ml myxin. Except for the lack of septation during the first 60 min, the filamentous forms appeared normal with well-defined nuclear bodies distributed throughout the cell.

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.

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