Protein Composition of the Cell Wall and Cytoplasmic Membrane of Escherichia coli
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TLDR
Envelope preparations obtained by passing Escherichia coli cells through a French pressure cell were separated by sucrose density gradient centrifugation into two distinct particulate fractions, and one of the proteins which is clearly localized in the cell wall is the protein with a molecular weight of 44,000, which is the major component of the envelope.Abstract:
Envelope preparations obtained by passing Escherichia coli cells through a French pressure cell were separated by sucrose density gradient centrifugation into two distinct particulate fractions. The fraction with the higher density was enriched in fragments derived from the cell wall, as indicated by the high content of lipopolysaccharide, the low content of cytochromes, and the similar morphology of the fragments and intact cell walls. The less-dense fraction was enriched in vesicles derived from the cytoplasmic membrane, as indicated by the enrichment of cytochromes, the enzymes lactic and succinic dehydrogenase and nitrate reductase, and the morphological similarity of the vesicles to intact cytoplasmic membrane. Both fractions were rich in phospholipid. The protein composition was compared by mixing the cytoplasmic membrane-enriched fraction from a (3)H-labeled culture with the cell wall-enriched fraction from a (14)C-labeled culture and examining the resulting mixture by gel electrophoresis. Thirty-four bands of radioactive protein were resolved; of these, 27 were increased two- to fourfold in the cytoplasmic membrane-enriched fraction, whereas 6 were similarly increased in the cell wall-enriched fraction. One of the proteins which is clearly localized in the cell wall is the protein with a molecular weight of 44,000, which is the major component of the envelope. This protein accounted for 70% of the total protein of the cell wall, and its occurrence in the envelope from spheroplasts suggests that it is a structural protein of the outer membranous component of the cell wall.read more
Citations
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Specific Removal of Proteins from the Envelope of Escherichia coli by Protease Treatments
Masayori Inouye,Mei-Lan Yee +1 more
TL;DR: When the envelope fraction of Escherichia coli was treated by trypsin, about 40% of total envelope proteins were removed from the fraction without changing its phospholipid content, while that of Pronase treatment was about 60%.
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Separation of inner and outer membranes of Rhodopseudomonas spheroides.
TL;DR: Th Thin sections of the vesicles of the inner membrane fraction and those of outer membrane provide morphological evidence for the identity of the individual membrane fractions.
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Epithelial cell adherence mediated by the enterotoxigenic Escherichia coli tia protein.
TL;DR: Results indicate that Tia is an invasin and adhesin that binds a specific receptor on HCT8 cells and predicts Tia to contain eight transmembrane amphipathic β-sheets with four loops exposed on the surface of the bacterial cell.
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Cell division in a chain-forming envA mutant of Escherichia coli K12. Fine structure of division sites and effects of EDTA, lysozyme and ampicillin.
TL;DR: It is suggested that the envA gene mediates a defect in the association of the murein skeleton with the outer layers of the envelope that separates individual cell units in a chain-forming envA mutant.
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Properties of membrane-associated sialyltransferase of Escherichia coli.
I K Vijay,F A Troy +1 more
TL;DR: Kinetic studies as well as sugar nucleotide, metal ion, pH, ammonium sulfate, and thiol reagent requirements showed these two complexes contained functionally identical enzymatic activities, and lipididity of the lipid phase is apparently required for proper function of this membraneassociated enzyme complex.
References
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Enzymatic properties of the inner and outer membranes of rat liver mitochondria
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Journal ArticleDOI
Chemical characterization, spatial distribution and function of a lipoprotein (murein-lipoprotein) of the E. coli cell wall. The specific effect of trypsin on the membrane structure.
Volkmar Braun,Kurt Rehn +1 more
TL;DR: It seems that cleavage of only one peptide bond adjacent to the lysine link between the lipoprotein and the murein causes the rapid decrease of the absorbance and as shown by electron microscopic exmination of ultrathin sections of trypsin treated cell walls, two separated membrane structures appear which otherwise are closely adjacent to one another.
Journal ArticleDOI
The location of the mucopeptide in sections of the cell wall of escherichia coli and other gram-negative bacteria
TL;DR: Electron micrographs of sections of Escherichia coli have shown that the wall has an extra component 20–30 A in thickness on the inside of the usual double-track profile, which is considered to contain the mucopeptide characteristic of bacteria.
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The rigid layer of the cell wall of Escherichia coli strain B.
W. Weidel,H. Frank,H. H. Martin +2 more
TL;DR: The structure conferring rigidity and shape on the complex cell wall of Escherichia coli strain B has been isolated in a state virtually free from other wall material and shows a characteristic surface pattern which indicates the fairly simple principles of its construction.
Journal ArticleDOI
Ultrastructure of the cell wall of Escherichia coli and chemical nature of its constituent layers
TL;DR: The chemical nature of the layers constituting the wall of E. coli was studied by examining the modifications induced in the ultrastructure of the wall by several enzymatic and chemical treatments, which could account for the available electron microscopic and chemical data.