scholarly journals Identification of the Escherichia coli cell division gene sep and organization of the cell division-cell envelope genes in the sep-mur-ftsA-envA cluster as determined with specialized transducing lambda bacteriophages.

1978 ◽  
Vol 133 (1) ◽  
pp. 91-100 ◽  
Author(s):  
G Fletcher ◽  
C A Irwin ◽  
J M Henson ◽  
C Fillingim ◽  
M M Malone ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Cell Division ◽  
Cell Envelope ◽  
Coli Cell ◽  
Division Cell

scholarly journals Two polypeptide products of the Escherichia coli cell division gene ftsW and a possible role for FtsW in FtsZ function.

1997 ◽  
Vol 179 (3) ◽  
pp. 784-793 ◽  
Author(s):  
M M Khattar ◽  
S G Addinall ◽  
K H Stedul ◽  
D S Boyle ◽  
J Lutkenhaus ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Cell Division ◽  
Coli Cell

scholarly journals Overexpression of lpxT Gene in Escherichia coli Inhibits Cell Division and Causes Envelope Defects without Changing the Overall Phosphorylation Level of Lipid A

2020 ◽  
Vol 8 (6) ◽  
pp. 826
Author(s):  
Federica A. Falchi ◽  
Flaviana Di Lorenzo ◽  
Roberto Pizzoccheri ◽  
Gianluca Casino ◽  
Moira Paroni ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Cell Division ◽  
Lipid A ◽  
Cell Envelope ◽  
Osmotic Shock ◽  
Ectopic Expression ◽  
Phenotypic Effect ◽  
Osmotic Lysis ◽  
Membrane Defects ◽  
Inner Membrane Protein

LpxT is an inner membrane protein that transfers a phosphate group from the essential lipid undecaprenyl pyrophosphate (C-55PP) to the lipid A moiety of lipopolysaccharide, generating a lipid A tris-phosphorylated species. The protein is encoded by the non-essential lpxT gene, which is conserved in distantly related Gram-negative bacteria. In this work, we investigated the phenotypic effect of lpxT ectopic expression from a plasmid in Escherichia coli. We found that lpxT induction inhibited cell division and led to the formation of elongated cells, mostly with absent or altered septa. Moreover, the cells became sensitive to detergents and to hypo-osmotic shock, indicating that they had cell envelope defects. These effects were not due to lipid A hyperphosphorylation or C-55PP sequestering, but most likely to defective lipopolysaccharide transport. Indeed, lpxT overexpression in mutants lacking the L,D-transpeptidase LdtD and LdtE, which protect cells with outer membrane defects from osmotic lysis, caused cell envelope defects. Moreover, we found that pyrophosphorylated lipid A was also produced in a lpxT deletion mutant, indicating that LpxT is not the only protein able to perform such lipid A modification in E. coli.

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