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By admin, on February 16th, 2012
By admin, on February 16th, 2012
Proc Natl Acad Sci U S A . 2012 Feb 13; Ricci DP, Hagan CL, Kahne D, Silhavy TJ The outer membrane (OM) of Gram-negative bacteria such as Escherichia coli contains lipoproteins and integral β-barrel proteins (outer-membrane proteins, OMPs) assembled into an asymmetrical lipid bilayer.
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Activation of the Escherichia coli β-barrel assembly machine (Bam) is required for essential components to interact properly with substrate.
By admin, on February 12th, 2012
Microbiology . 2012 Feb 9; Shiba Y, Miyagawa H, Nagahama H, Matsumoto K, Kondo D, Matsuoka S, Matsumoto K, Hara H The Rcs phosphorelay signal transduction system controls genes for capsule production and many other envelope-related functions and is implicated in biofilm formation. We investigated the activation of the Rcs system in a pgsA null mutant of Escherichia coli, which completely lacks the major acidic phospholipids, phosphatidylglycerol and cardiolipin.
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Exploring the relationship between lipoprotein mislocalisation and activation of the Rcs signal transduction system in Escherichia coli.
By admin, on February 12th, 2012
Microbiology . 2012 Feb 9; Shiba Y, Miyagawa H, Nagahama H, Matsumoto K, Kondo D, Matsuoka S, Matsumoto K, Hara H The Rcs phosphorelay signal transduction system controls genes for capsule production and many other envelope-related functions and is implicated in biofilm formation. We investigated the activation of the Rcs system in a pgsA null mutant of Escherichia coli, which completely lacks the major acidic phospholipids, phosphatidylglycerol and cardiolipin.
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Exploring the relationship between lipoprotein mislocalisation and activation of the Rcs signal transduction system in Escherichia coli.
By admin, on February 6th, 2012
Langmuir . 2012 Feb 2; Sharma KS, Durand G, Gabel F, Bazzacco P, Le Bon C, Billon-Denis E, Catoire LJ, Popot JL, Ebel C, Pucci B A novel type of non-ionic amphipols for handling membrane proteins in detergent-free aqueous solutions has been obtained through free-radical homotelomerization of an acrylamide-based monomer comprising a C11 alkyl chain and two glucose moieties, using a thiol as transfer reagent. By controlling the thiol/monomer ratio, the number-average molecular weight of the polymers was varied from 8 to 63 kDa.
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Non-Ionic Amphiphilic Homopolymers: Synthesis, Solution Properties and Biochemical Validation.
By admin, on February 6th, 2012
Langmuir . 2012 Feb 2; Sharma KS, Durand G, Gabel F, Bazzacco P, Le Bon C, Billon-Denis E, Catoire LJ, Popot JL, Ebel C, Pucci B A novel type of non-ionic amphipols for handling membrane proteins in detergent-free aqueous solutions has been obtained through free-radical homotelomerization of an acrylamide-based monomer comprising a C11 alkyl chain and two glucose moieties, using a thiol as transfer reagent.
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Non-Ionic Amphiphilic Homopolymers: Synthesis, Solution Properties and Biochemical Validation.
By admin, on February 5th, 2012
Diagn Microbiol Infect Dis . 2012 Jan 31; Van der Bij AK, Peirano G, Pitondo-Silva A, Pitout JD Successful international clones have recently emerged among Escherichia coli that produce CTX-M β-lactamases as important causes of community-onset urinary tract and bloodstream infections.
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The presence of genes encoding for different virulence factors in clonally related Escherichia coli that produce CTX-Ms.
By admin, on February 1st, 2012
Abstract Micro integral membrane protein (MIMP) has been shown to adhere to mucin and antagonize the adhesion of enteropathogenic Escherichia coli (EPEC) to epithelial cells, however, the mechanism has not been fully …
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Involvement of mannose receptor and the p38 MAPK signaling …
By admin, on January 29th, 2012
By admin, on January 29th, 2012
By admin, on January 28th, 2012
Acta Crystallogr D Biol Crystallogr . 2012 Feb; 68(Pt 2): 95-101 Dong C, Hou HF, Yang X, Shen YQ, Dong YH The outer membrane protein complex (BAM complex) plays an important role in outer membrane protein (OMP) assembly in Escherichia coli. The BAM complex includes the integral β-barrel protein BamA as well as four lipoproteins: BamB, BamC, BamD and BamE
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Structure of Escherichia coli BamD and its functional implications in outer membrane protein assembly.
By admin, on January 21st, 2012
Genes Cells . 2012 Jan 18; Murata M, Noor R, Nagamitsu H, Tanaka S, Yamada M A large number of Escherichia coli cells become viable but nonculturable at early stationary phase, most of which are directed to lysis in cells with an enhanced active σ(E) level.
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Novel pathway directed by σ(E) to cause cell lysis in Escherichia coli.
By admin, on January 21st, 2012
Genes Cells . 2012 Jan 18; Murata M, Noor R, Nagamitsu H, Tanaka S, Yamada M A large number of Escherichia coli cells become viable but nonculturable at early stationary phase, most of which are directed to lysis in cells with an enhanced active σ(E) level. In this study, we examined the effect of small noncoding RNAs, MicA and RybB, as σ(E) regulon as well as regulators of outer membrane protein (Omp) genes, on the lysis process
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Novel pathway directed by σ(E) to cause cell lysis in Escherichia coli.
By admin, on January 19th, 2012
FEBS J . 2012 Jan 17; Reusch RN Outer membrane protein A (OmpA) of Escherichia coli is a paradigm for the biogenesis of outer membrane proteins; however, the structure and assembly of OmpA have remained controversial. A review of studies to date supports the hypothesis that native OmpA is a single-domain large pore, while a two-domain narrow pore structure is a folding intermediate or minor conformer
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Insights into the Structure and Assembly of Escherichia coli Outer Membrane Protein A.
By admin, on January 18th, 2012
By admin, on January 18th, 2012
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