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Assembly of Bacterial Outer Membrane Proteins
2012Various methods that are routinely used to study the subcellular localization of membrane proteins in wild-type Gram-negative bacteria fall short in genetic studies addressing the biogenesis of outer membrane proteins (OMPs). Here, we describe three biochemical methods that can be used in such studies to evaluate the proper assembly of OMPs into the ...
Grijpstra, J. +2 more
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Structural Aspects of Bacterial Outer Membrane Protein Assembly
2015The outer membrane of Gram-negative bacteria is predominantly populated by β-Barrel proteins and lipid anchored proteins that serve a variety of biological functions. The proper folding and assembly of these proteins is essential for bacterial viability and often plays a critical role in virulence and pathogenesis. The β-barrel assembly machinery (Bam)
Charles, Calmettes +2 more
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Outer Membrane Protein OmpB Methylation May Mediate Bacterial Virulence
Trends in Biochemical Sciences, 2017Methylation of outer membrane proteins (OMPs) has been implicated in bacterial virulence. Lysine methylation in rickettsial OmpB is correlated with rickettsial virulence, and N- and O-methylations are also observed in virulence-relevant OMPs from several pathogenic bacteria that cause typhus, leptospirosis, tuberculosis, and anaplasmosis.
David C H, Yang +4 more
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Bacterial ß-Barrel Outer Membrane Proteins
2009ß-barrel outer membrane proteins constitute the second and less well-studied class of transmembrane proteins. They are present exclusively in the outer membrane of Gram-negative bacteria and presumably in the outer membrane of mitochondria and chloroplasts.
Pantelis G. Bagos, Stavros J. Hamodrakas
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Modeling and simulation of bacterial outer membranes and interactions with membrane proteins
Current Opinion in Structural Biology, 2017The outer membrane (OM) of Gram-negative bacteria is composed of phospholipids in the periplasmic leaflet and lipopolysaccharides (LPS) in the external leaflet, along with β-barrel OM proteins (OMPs) and lipidated periplasmic lipoproteins. As a defensive barrier to toxic compounds, an LPS molecule has high antigenic diversity and unique combination of ...
Dhilon S Patel, Yifei Qi, Wonpil Im
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Multiple pathways allow protein secretion across the bacterial outer membrane
Current Opinion in Cell Biology, 2000Secretion of proteins across the bacterial outer membrane takes place via a variety of mechanisms from simple one-component systems to complex multicomponent pathways. Secretion pathways can be organized into evolutionarily and functionally related groups, which highlight their relationship with organelle biogenesis.
D G, Thanassi, S J, Hultgren
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Bacterial outer membrane protein analysis by electrophoresis and microchip technology
Expert Review of Proteomics, 2007Outer membrane proteins are indispensable components of bacterial cells and participate in several relevant functions of the microorganisms. Changes in the outer membrane protein composition might alter antibiotic sensitivity and pathogenicity. Furthermore, the effects of various factors on outer membrane protein expression, such as antibiotic ...
Ildikó, Kustos +2 more
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Biogenesis of β-barrel integral proteins of bacterial outer membrane
Biochemistry (Moscow), 2012Gram-negative bacteria are enveloped by two membranes, the inner (cytoplasmic) (CM) and the outer (OM). The majority of integral outer membrane proteins are arranged in β-barrels of cylindrical shape composed of amphipathic antiparallel β-strands. In bacteria, β-barrel proteins function as water-filled pores, active transporters, enzymes, receptors ...
T F, Solov'eva +2 more
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Nature, 1986
The LamB protein is an integral membrane protein of the outer membrane of Escherichia coli. We have now found that, when synthesized in an E. coli cell-free translation system supplemented with inverted vesicles derived from the E. coli inner membrane, LamB protein is integrated into the vesicle membrane as assayed by its resistance to extraction at ...
M, Watanabe, J F, Hunt, G, Blobel
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The LamB protein is an integral membrane protein of the outer membrane of Escherichia coli. We have now found that, when synthesized in an E. coli cell-free translation system supplemented with inverted vesicles derived from the E. coli inner membrane, LamB protein is integrated into the vesicle membrane as assayed by its resistance to extraction at ...
M, Watanabe, J F, Hunt, G, Blobel
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Omp85, an evolutionarily conserved bacterial protein involved in outer-membrane-protein assembly
Research in Microbiology, 2004The insertion of proteins into membranes generally requires the assistance of membrane proteins. A protein, designated Omp85 in Neisseria meningitidis, was shown to be required for the assembly of bacterial outer-membrane proteins. The protein is essential for the viability of the bacteria and is ubiquitous among Gram-negative bacteria. Omp85 depletion
Voulhoux, J.R., Tommassen, J.P.M.
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