Modulation of mitochondrial apoptosis by PI3K inhibitors.

Mitochondrion . 2012 May 9; Fulda S Most anticancer therapies exert their action by triggering programmed cell death (apoptosis) in cancer cells. The mitochondrial pathway of apoptosis is initiated by mitochondrial outer membrane permeabilization, leading to the release of apoptogenic factors such as cytochrome c or Smac from the mitochondrial intermembrane space into the cytosol.

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Modulation of mitochondrial apoptosis by PI3K inhibitors.

Construction of iucB and iucBiutA mutants of avian pathogenic Escherichia coli and evaluation of their pathogenicity.

Vet Microbiol. 2012 Apr 25;
Xiong L, Ling J, Gao Q, Zhou Y, Li T, Gao S, Liu X

Aerobactin counts for much to the pathogenesis of avian pathogenic Escherichia coli (APEC), iutA is responsible for the expression of a specific outer membrane receptor protein for ferric aerobactin, and iucB is involved in the aerobactin synthesis. To our knowledge, the contribution of iucB to the pathogenicity of APEC has not been assessed till now. In this study, the mutants E058ΔiucB and E058ΔiucBΔiutA were constructed and characterized. There were no differences observed in a series of tests including the embryo lethality, invasion assay in HD11 cells and the ability to survive in SPF chicken serum. Meanwhile, the mutants showed decreased pathogenicity as compared with the wild-type strain through a series of experiments in vivo. The mutants E058ΔiucB and E058ΔiucBΔiutA greatly reduced in all of the tested tissues in vivo persistence (p<0.001). In the meantime, the mutants had no ability to produce aerobactin. Reintroduction of the iucB gene on a multicopy expression plasmid pGEX-6p-1 restored the capacity to produce aerobactin as similar to that of wild-type strain E058. The results indicated that the iucB gene related virulence factors including the iron assimilation system were important for the pathogenesis of APEC E058. As showed in the in vivo competition assay, compared to the parental strain E058, E058ΔiucB had a significant reduction of bacterial loads in heart (p<0.01), liver (p<0.01), kidney (p<0.01), spleen (p<0.05) and lung (p<0.05), respectively, while E058ΔiucBΔiutA had a sharp reduction in all of the five tissues to be tested (p<0.001). These results suggested that the single gene either iucB or iutA was likely to be involved directly or indirectly in iron uptake for the pathogenicity of APEC E058, and there was an obviously synergistic effect between iucB and iutA genes on the pathogenicity of APEC E058.

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Construction of iucB and iucBiutA mutants of avian pathogenic Escherichia coli and evaluation of their pathogenicity.

Genetic, Biochemical, and Molecular Characterization of the BamA POTRA Domain of Escherichia coli.

J Bacteriol . 2012 Apr 27; Workman P, Heidi K, Giuliano N, Lee N, Mar J, Vuong P, Bennion D, Misra R The BamA protein of Escherichia coli plays a central role in the assembly of β-barrel outer membrane proteins (OMPs). The C-terminus domain of BamA folds into an integral outer membrane β-barrel and the N-terminus forms a periplasmic polypeptide transport-associated (POTRA) domain for OMP reception and assembly.

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Genetic, Biochemical, and Molecular Characterization of the BamA POTRA Domain of Escherichia coli.

The bacterial outer membrane β-barrel assembly machinery.

Protein Sci . 2012 Mar 30; Kim KH, Aulakh S, Paetzel M β-Barrel proteins found in the outer membrane of Gram-negative bacteria serve a variety of cellular functions. Proper folding and assembly of these proteins are essential for the viability of bacteria and can also play an important role in virulence

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The bacterial outer membrane β-barrel assembly machinery.

Pink1 and its {Delta}ψ-dependent cleavage product both localize to the outer mitochondrial membrane by a unique targeting mode.

J Biol Chem . 2012 Apr 30; Becker D, Richter J, Tocilescu MA, Przedborski S, Voos W The Parkinson`s disease-associated kinase Pink1 is targeted to mitochondria where it is thought to regulate mitochondrial quality control by promoting the selective autophagic removal of dysfunctional mitochondria. Nevertheless, the targeting mode of Pink1 and its submitochondrial localization are still not conclusively resolved

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Pink1 and its {Delta}ψ-dependent cleavage product both localize to the outer mitochondrial membrane by a unique targeting mode.

@NadoAPBio what protein pumps hydrogens between the space between the inner and outer membrane? #apbioreview #apbioreview

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@NadoAPBio what protein pumps hydrogens between the space between the inner and outer membrane? #apbioreview #apbioreview

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VirK is a Periplasmic Protein Required for Efficient Secretion of Pet from Enteroaggregative E. coli.

Infect Immun . 2012 Apr 30; Tapia-Pastrana G, Chavez-Dueñas L, Lanz-Mendoza H, Teter K, Navarro-Garcia F Despite the autotransporter (AT) moniker, AT secretion appears to involve the function of periplasmic chaperones. We identified four periplasmic proteins that specifically bound to plasmid-encoded toxin (Pet), an AT produced by enteroaggregative Escherichia coli (EAEC).

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VirK is a Periplasmic Protein Required for Efficient Secretion of Pet from Enteroaggregative E. coli.

Predicting the outer membrane proteome of Pasteurella multocida …

Predicting the outer membrane proteome of Pasteurella multocida based on consensus prediction enhanced by results integration and manual confirmation. Outer membrane proteins (OMPs) of Pasteurella multocida have

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Predicting the outer membrane proteome of Pasteurella multocida …

Immunologische und molekularbiologische Untersuchungen des outer membrane protein A von Proteus mirabilis: Mit b… http://t.co/nbuBmmPu

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HmuP is a co-activator of Irr-dependent expression of heme utilization genes in Bradyrhizobium japonicum.

J Bacteriol . 2012 Apr 13; Escamilla-Hernandez R, O’Brian MR Utilization of heme as an iron source by Bradyrhizobium japonicum involves induction of the outer membrane heme receptor gene hmuR and other genes within the heme utilization locus. Here, we discovered the hmuP gene located upstream of hmuR and transcribed divergently from it along with hmuTUV

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HmuP is a co-activator of Irr-dependent expression of heme utilization genes in Bradyrhizobium japonicum.

E. coli LoiP (YggG), a metalloprotease hydrolyzing Phe-Phe bonds.

Mol Biosyst . 2012 Apr 11; Lütticke C, Hauske P, Lewandrowski U, Sickmann A, Kaiser M, Ehrmann M YggG is a conserved lipoprotein localized to the outer membrane of Gram negative bacteria. Even though the expressed open reading frame has been identified previously, the Escherichia coli protein remained uncharacterized.

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E. coli LoiP (YggG), a metalloprotease hydrolyzing Phe-Phe bonds.

Expression and Immunogenicity Analysis of Outer Membrane …

Mathematics · Geophysics · Physics · Biological · Geology · Resources Science · System Sscience · Home » Basic Science » Expression and Immunogenicity Analysis of Outer Membrane Protein of Actinobacillus Pleuropneumoniae it's antibody titer(anti-ApxⅡ) is higher;And the protective rates of groupâ…¡I and groupâ…¤seem better than others.The results revealed that these outer membrane proteins of App play an important role in protect from attacking of App.

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Expression and Immunogenicity Analysis of Outer Membrane …

Expression and Immunogenicity Analysis of Outer Membrane …

Mathematics · Geophysics · Physics · Biological · Geology · Resources Science · System Sscience · Home » Basic Science » Expression and Immunogenicity Analysis of Outer Membrane Protein of Actinobacillus Pleuropneumoniae it's antibody titer(anti-ApxⅡ) is higher;And the protective rates of groupâ…¡I and groupâ…¤seem better than others.The results revealed that these outer membrane proteins of App play an important role in protect from attacking of App.

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Expression and Immunogenicity Analysis of Outer Membrane …

http://t.co/8YDJFngP Alp, an Arthropod-Associated Outer Membrane Protein of Borrelia Species That Cause Relapsing Fever http://t.co/toucCugQ

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http://t.co/8YDJFngP Alp, an Arthropod-Associated Outer Membrane Protein of Borrelia Species That Cause Relapsing Fever http://t.co/toucCugQ

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