Protein Complexes of the Escherichia coli Cell Envelope
نویسندگان
چکیده
منابع مشابه
Fracture faces in the cell envelope of Escherichia coli.
Freeze-fracturing of Escherichia coli cells in the presence of 30% (v/v) glycerol resulted in a double cleavage of the cell envelope exposing two convex and two concave fracture faces ([Formula: see text], [Formula: see text] and [Formula: see text], [Formula: see text]) with characteristic patterns. Complementary replicas revealed the relationship of the fracture faces to their corresponding f...
متن کاملEffect of the inhibition of protein synthesis on the Escherichia coli cell envelope.
The consequences for cell envelope integrity of Escherichia coli K-12 of the inhibition of protein synthesis by a variety of means have been examined. Protein synthesis was blocked by the antibiotics chloramphenicol and streptomycin, by amino acid starvation of an amino acid auxotroph, and by inactivation of temperature-sensitive aminoacyl transfer ribonucleic acid synthetase and ribosomal muta...
متن کاملGenetic analysis of 15 protein folding factors and proteases of the Escherichia coli cell envelope.
Each cell hosts thousands of proteins that vary greatly in abundance, structure, and chemical properties. To ensure that all proteins are biologically active and properly localized, efficient quality control systems have evolved. While the structure, function, and regulation of some individual protein folding factors and proteases were resolved up to atomic resolution, others remain poorly char...
متن کاملCell envelope and shape of Escherichia coli K12.
Rod-shaped "ghosts" that are free of murein have been isolated from E. coli. The shape of these "ghosts" is maintained by a unit membrane soluble in sodium dodecyl sulfate. Ghosts consist of about 20-30% phospholipid (almost exclusively phosphatidylethanolamine) and 50-60% protein; a large fraction of the remaining material is lipopolysaccharide. Sodium dodecyl sulfate-gel electrophoresis revea...
متن کاملEscherichia coli strains blocked in Tat-dependent protein export exhibit pleiotropic defects in the cell envelope.
The Tat system is a recently discovered protein export pathway that serves to translocate folded proteins, often containing redox cofactors, across the bacterial cytoplasmic membrane. Here we report that tat strains are associated with a mutant cell septation phenotype, where chains of up to 10 cells are evident. Mutant strains are also hypersensitive to hydrophobic drugs and to lysis by lysozy...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2005
ISSN: 0021-9258
DOI: 10.1074/jbc.m506479200