|
|
By admin, on May 15th, 2012
Open Biochem J. 2012; 6: 40-2
Contag B
A new hypothesis is discussed, which describes the initiation of the carcinogenesis through polycyclic aromatic hydrocarbons (PAHs) and aminoazo dyes (AZOs) as a two-step process: the oncogenic proteins of the ras or ras-like on-cogenes activated by mutation (“initiation A “) co-operate with the complexes in the plasma membrane formed during the “initiation B ” stage from the parent compounds of the PAHs or AZOs with cholesterol and apolipoprotein A-I. The final result of this co-operation, or the “complete initiation”, is an irreversibly modified membrane architecture with negative consequences for growth control.
Go here to read the rest:
Hypothetical two-step initiation of experimental carcinogenesis by polycyclic aromatic hydrocarbons and aminoazo dyes.
By admin, on May 3rd, 2012
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.
See the original post:
The bacterial outer membrane β-barrel assembly machinery.
By admin, on April 28th, 2012
Protein Expr Purif . 2012 Apr 17; Roussel G, Matagne A, De Bolle X, Perpète EA, Michaux C Brucella melitensis is a gram-negative bacteria known to cause brucellosis and to produce severe infections in humans.
Follow this link:
Purification, refolding and characterization of the trimeric Omp2a outer membrane porin from Brucella melitensis.
By admin, on April 28th, 2012
Protein Expr Purif . 2012 Apr 17; Roussel G, Matagne A, De Bolle X, Perpète EA, Michaux C Brucella melitensis is a gram-negative bacteria known to cause brucellosis and to produce severe infections in humans. Whilst brucella’s outer membrane proteins have been extensively studied due to their potential role as antigens or virulence factors, their function is still poorly understood at the structural level, as the 3D structure of Brucella β-barrel membrane proteins are still unknown
Excerpt from:
Purification, refolding and characterization of the trimeric Omp2a outer membrane porin from Brucella melitensis.
By admin, on April 24th, 2012
J Biol Chem . 2012 Apr 20; Wang X, Pineau C, Gu S, Guschinskaya N, Pickersgill RW, Shevchik VE The type II secretion system (T2SS) secretes enzymes and toxins across the outer membrane of Gram-negative bacteria. The precise assembly of T2SS, which consists of at least twelve core-components called Gsp, remains unclear
Read more:
Cysteine scanning mutagenesis and disulfide mapping analysis of the arrangement of GspC and GspD protomers within the T2SS.
By admin, on April 19th, 2012
J Bacteriol . 2012 Apr 13; Kustusch RJ, Kuehl CJ, Crosa JH The TonB system of proteins is required for the energy dependent active transport of iron bound substrates across the outer membrane of gram-negative bacteria. We have identified three TonB systems within the human pathogen V
Link:
Three TonB systems in the human pathogen Vibrio vulnificus: two contain the ttpC gene but only one of them is active in iron transport and virulence.
By admin, on April 19th, 2012
J Bacteriol . 2012 Apr 13; Kustusch RJ, Kuehl CJ, Crosa JH The TonB system of proteins is required for the energy dependent active transport of iron bound substrates across the outer membrane of gram-negative bacteria. We have identified three TonB systems within the human pathogen V.
Read more:
Three TonB systems in the human pathogen Vibrio vulnificus: two contain the ttpC gene but only one of them is active in iron transport and virulence.
By admin, on April 17th, 2012
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.
Continued here:
E. coli LoiP (YggG), a metalloprotease hydrolyzing Phe-Phe bonds.
By admin, on April 16th, 2012
J Bacteriol . 2012 Apr 6; Ollis AA, Postle K In Gram negative bacteria, the cytoplasmic membrane protonmotive force energizes active transport of TonB-dependent ligands through outer membrane TonB-gated transporters. In Escherichia coli, cytoplasmic membrane proteins ExbB and ExbD couple the protonmotive force to conformational changes in TonB, which are hypothesized to form the basis of energy transduction through direct contact with the transporters.
See the original post:
Identification of Functionally Important TonB-ExbD Periplasmic Domain Interactions in vivo.
By admin, on April 16th, 2012
J Bacteriol . 2012 Apr 6; Ollis AA, Postle K In Gram negative bacteria, the cytoplasmic membrane protonmotive force energizes active transport of TonB-dependent ligands through outer membrane TonB-gated transporters. In Escherichia coli, cytoplasmic membrane proteins ExbB and ExbD couple the protonmotive force to conformational changes in TonB, which are hypothesized to form the basis of energy transduction through direct contact with the transporters.
Link:
Identification of Functionally Important TonB-ExbD Periplasmic Domain Interactions in vivo.
By admin, on April 15th, 2012
J Bacteriol . 2012 Apr 6; Ollis AA, Kumar A, Postle K The TonB system of Gram negative bacteria energizes active transport of diverse nutrients through high-affinity TonB-gated outer membrane transporters using energy derived from the cytoplasmic membrane protonmotive force.
Read the original here:
The ExbD Periplasmic Domain Contains Distinct Functional Regions for Two Stages in TonB Energization.
By admin, on April 14th, 2012
Biochemistry . 2012 Apr 12; Flores Jimenez RH, Cafiso DS Gram-negative bacteria contain a family of outer membrane transport proteins that function in the uptake of rare nutrients, such as iron and vitamin B12.
See the original post:
The N-terminal Domain of a TonB-dependent Transporter Undergoes a Reversible Stepwise Denaturation.
By admin, on April 14th, 2012
Biochemistry . 2012 Apr 12; Flores Jimenez RH, Cafiso DS Gram-negative bacteria contain a family of outer membrane transport proteins that function in the uptake of rare nutrients, such as iron and vitamin B12. These proteins are termed TonB-dependent because transport requires an interaction with the inner membrane protein TonB.
Go here to see the original:
The N-terminal Domain of a TonB-dependent Transporter Undergoes a Reversible Stepwise Denaturation.
By admin, on April 7th, 2012
By admin, on April 7th, 2012
Nat Rev Microbiol . 2012 Apr 2; Korotkov KV, Sandkvist M, Hol WG Many Gram-negative bacteria use the sophisticated type II secretion system (T2SS) to translocate a wide range of proteins from the periplasm across the outer membrane. The inner-membrane platform of the T2SS is the nexus of the system and orchestrates the secretion process through its interactions with the periplasmic filamentous pseudopilus, the dodecameric outer-membrane complex and a cytoplasmic secretion ATPase
Here is the original post:
The type II secretion system: biogenesis, molecular architecture and mechanism.
By admin, on March 20th, 2012
Curr Top Microbiol Immunol . 2012 Mar 20; Kubatzky KF Pasteurella multocida was first discovered by Perroncito in 1878 and named after Louis Pasteur who first isolated and described this Gram-negative bacterium as the cause of fowl disease in 1880. Subsequently, P.
Continued here:
Pasteurella Multocida and Immune Cells.
|
