Results 11 to 20 of about 128,512 (289)

Overproducing the BAM complex improves secretion of difficult-to-secrete recombinant autotransporter chimeras. [PDF]

open access: goldMicrob Cell Fact, 2021
AbstractMonomeric autotransporters have been used extensively to transport recombinant proteins or protein domains to the cell surface of Gram-negative bacteria amongst others for antigen display. Genetic fusion of such antigens into autotransporters has yielded chimeras that can be used for vaccination purposes.
Phan TH   +5 more
europepmc   +9 more sources

Darobactin B Stabilises a Lateral-Closed Conformation of the BAM Complex in E. coli Cells. [PDF]

open access: hybridAngew Chem Int Ed Engl, 2023
AbstractThe β‐barrel assembly machinery (BAM complex) is essential for outer membrane protein (OMP) folding in Gram‐negative bacteria, and represents a promising antimicrobial target. Several conformational states of BAM have been reported, but all have been obtained under conditions which lack the unique features and complexity of the outer membrane ...
Haysom SF   +11 more
europepmc   +9 more sources

Classifying β-Barrel Assembly Substrates by Manipulating Essential Bam Complex Members. [PDF]

open access: bronzeJ Bacteriol, 2016
ABSTRACT The biogenesis of the outer membrane (OM) of Escherichia coli is a conserved and vital process. The assembly of integral β-barrel outer membrane proteins (OMPs), which represent a major component of the OM, depends on periplasmic chaperones and the heteropentameric β-barrel assembly machine (Bam ...
Mahoney TF, Ricci DP, Silhavy TJ.
europepmc   +6 more sources

Discovery of a distinct BAM complex in the Bacteroidetes

open access: gold
AbstractThe BAM (β-barrel assembly machinery) complex is an evolutionarily conserved, multiprotein machine that catalyses the folding and membrane insertion of newly synthesised β-barrel outer membrane (OM) proteins in Gram-negative bacteria. Based on Proteobacteria, bacterial BAM is also structurally conserved, with an essential BamAD core and up to ...
Silale A   +10 more
europepmc   +3 more sources

An In Vitro Assay for Outer Membrane Protein Assembly by the BAM Complex. [PDF]

open access: greenMethods Mol Biol, 2015
To elucidate the mechanism of a biochemical process it is often essential to reconstitute the reaction in vitro using the minimal set of factors required to drive the reaction to completion. Here, we describe a method to reconstitute the folding and membrane integration of bacterial outer membrane (OM) proteins that have a characteristic β-barrel ...
Roman-Hernandez G, Bernstein HD.
europepmc   +6 more sources

Assembly of Outer Membrane β-Barrel Proteins: the Bam Complex. [PDF]

open access: greenEcoSal Plus, 2011
The major class of integral proteins found in the outer membrane (OM) of E. coli and Salmonella adopt a β-barrel conformation (OMPs). OMPs are synthesized in the cytoplasm with a typical signal sequence at the amino terminus, which directs them to the secretion machinery (SecYEG) located in ...
Malinverni JC, Silhavy TJ.
europepmc   +6 more sources

A modular BAM complex in the outer membrane of the alpha-proteobacterium Caulobacter crescentus. [PDF]

open access: yesPLoS ONE, 2010
Mitochondria are organelles derived from an intracellular alpha-proteobacterium. The biogenesis of mitochondria relies on the assembly of beta-barrel proteins into the mitochondrial outer membrane, a process inherited from the bacterial ancestor ...
Khatira Anwari   +11 more
doaj   +5 more sources

Reconstitution of Bam Complex-Mediated Assembly of a Trimeric Porin into Proteoliposomes. [PDF]

open access: yesmBio, 2021
Porins are a widespread family of homotrimers that represent a substantial fraction of the total protein located in the OM of many proteobacteria. These proteins facilitate the nonspecific diffusion of small molecules across the outer membrane and strongly influence the susceptibility of bacteria to clinically used antibiotics.
Hussain S, Peterson JH, Bernstein HD.
europepmc   +4 more sources

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