scholarly journals Penicillin-insensitive incorporation of D-amino acids into cell wall peptidoglycan influences the amount of bound lipoprotein in Escherichia coli.

1984 ◽  
Vol 160 (3) ◽  
pp. 889-894 ◽  
Author(s):  
T Tsuruoka ◽  
A Tamura ◽  
A Miyata ◽  
T Takei ◽  
K Iwamatsu ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Amino Acids ◽  
Cell Wall ◽  
Cell Wall Peptidoglycan

scholarly journals Recycling of the Anhydro-N-Acetylmuramic Acid Derived from Cell Wall Murein Involves a Two-Step Conversion to N-Acetylglucosamine-Phosphate

2005 ◽  
Vol 187 (11) ◽  
pp. 3643-3649 ◽  
Author(s):  
Tsuyoshi Uehara ◽  
Kyoko Suefuji ◽  
Noelia Valbuena ◽  
Brian Meehan ◽  
Michael Donegan ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Amino Acids ◽  
Cell Wall ◽  
Deletion Mutant ◽  
Biosynthetic Pathway ◽  
Reverse Genetics ◽  
Side Wall ◽  
Cell Extract ◽  
Amino Sugars ◽  
Kinase Gene

ABSTRACT Escherichia coli breaks down over 60% of the murein of its side wall and reuses the component amino acids to synthesize about 25% of the cell wall for the next generation. The amino sugars of the murein are also efficiently recycled. Here we show that the 1,6-anhydro-N-acetylmuramic acid (anhMurNAc) is returned to the biosynthetic pathway by conversion to N-acetylglucosamine-phosphate (GlcNAc-P). The sugar is first phosphorylated by anhydro- N -acetylmuramic acid kinase (AnmK), yielding MurNAc-P, and this is followed by action of an etherase which cleaves the bond between d-lactic acid and the N-acetylglucosamine moiety of MurNAc-P, yielding GlcNAc-P. The kinase gene has been identified by a reverse genetics method. The enzyme was overexpressed, purified, and characterized. The cell extract of an anmK deletion mutant totally lacked activity on anhMurNAc. Surprisingly, in the anmK mutant, anhMurNAc did not accumulate in the cytoplasm but instead was found in the medium, indicating that there was rapid efflux of free anhMurNAc.

Release of D-alanyl-D-alanine from the precursor of the cell wall peptidoglycan by a peptidase of Escherichia coli K 12

Biochimie ◽  
1973 ◽  
Vol 55 (6-7) ◽  
pp. 685-691 ◽  
Author(s):  
Bernard Gondré ◽  
Bernard Flouret ◽  
Jean van Heijenoort
Keyword(s):  
Escherichia Coli ◽  
Cell Wall ◽  
Cell Wall Peptidoglycan ◽  
K 12

Haemophilus vaginalis 594, a Gram-negative organism?

1971 ◽  
Vol 17 (7) ◽  
pp. 865-869 ◽  
Author(s):  
B. Sue Criswell ◽  
Judith H. Marston ◽  
Wayne A. Stenback ◽  
S. H. Black ◽  
Herman L. Gardner
Keyword(s):  
Escherichia Coli ◽  
Amino Acids ◽  
Cell Wall ◽  
Bacillus Megaterium ◽  
Teichoic Acid ◽  
Biochemical Properties ◽  
Positive Bacterium ◽  
Gram Negative ◽  
Bacterium Bacillus ◽  
Escherichia Coli B

The fine structure of Haemophilus vaginalis 594 (ATCC 14018) was examined by electron microscopy, and the biochemical composition of its cell wall was determined. For comparison, similar studies were done with a Gram-positive bacterium, Bacillus megaterium KM, and a Gram-negative bacterium, Escherichia coli B. Both Haemophilus vaginalis 594 and Escherichia coli B possessed a multiple-layered cell wall containing 11 to 14 amino acids, a low mucopeptide content, and no teichoic acid. In contrast, Bacillus megaterium KM had a thick, amorphous cell wall with five amino acids, high mucopeptide content, and detectable amounts of teichoic acid. Haemophilus vaginalis 594 resembled Escherichia coli, a member of the Gram-negative group of organisms. The structural and biochemical properties of Haemophilus vaginalis, which are described in detail, may prove useful in determining the ultimate taxonomic position of this species.

scholarly journals Boosting Secretion of Extracellular Protein byEscherichia colivia Cell Wall Perturbation

2018 ◽  
Vol 84 (20) ◽  
Author(s):  
Haiquan Yang ◽  
Xiao Lu ◽  
Jinyuan Hu ◽  
Yuan Chen ◽  
Wei Shen ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Cell Wall ◽  
Protein Secretion ◽  
Extracellular Protein ◽  
Deletion Mutants ◽  
Cell Factory ◽  
Content Type ◽  
E Coli ◽  
Cell Wall Peptidoglycan ◽  
Extracellular Secretion

ABSTRACTEscherichia coliis one of the most widely used host microorganisms for recombinant protein expression and metabolic engineering, but it cannot efficiently secrete recombinant proteins to extracellular space. Here, extracellular protein secretion was enhanced inE. coliby deleting twod,d-carboxypeptidase genes (dacAanddacB, single and double deletions) to perturb the cell wall peptidoglycan network. Deletion ofdacAanddacBenhanced the accumulation of intracellular soluble peptidoglycan inE. coliand affected cell morphology, resulting in a more irregular cell shape and the appearance of transparent bulges. Deletion ofdacAanddacBappears to disrupt the normal rigid structure, presumably due to perturbation and destruction of the cell wall peptidoglycan network. The extracellular green fluorescent protein (GFP) fluorescence intensity of deletion mutants was increased by >2.0-fold compared with that of control cells, and that of the double deletion mutant was increased by 2.7-fold. Extracellular recombinant fibroblast growth factor receptor 2 (FGFR2) and collagen E4 secretion in deletion mutants was also enhanced compared with that in the control cells. Additionally, the extracellular recombinant amylase activity of single-deletion mutants BL21 ΔdacApETDuet-amykand BL21 ΔdacBpETDuet-amykwas increased 2.5- and 3.1-fold, respectively. The extracellular distribution of α-galactosidase by deletion mutants was also increased by >2.0-fold. Deletion ofdacAanddacBincreased outer membrane permeability, which could explain the enhanced extracellular protein secretion.IMPORTANCECell surface structure stabilization is important for extracellular secretion of proteins inEscherichia coli. As the main constituent of the cell wall, peptidoglycan contributes to cell structure robustness and stability. Here, we perturbed the peptidoglycan network by deletingdacAanddacBgenes encodingd,d-carboxypeptidase enzymes to improve extracellular protein secretion. This new strategy could enhance the capacity ofE. colias a microbial cell factory for extracellular secretion of proteins and chemicals.

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