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Journal articles on the topic 'Outer membrane proteins'

Author: Grafiati

Published: 4 June 2021

Last updated: 28 January 2023

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1

Ishikawa, Daigo, Hayashi Yamamoto, Yasushi Tamura, Kaori Moritoh, and Toshiya Endo. "Two novel proteins in the mitochondrial outer membrane mediate β-barrel protein assembly." Journal of Cell Biology 166, no. 5 (August 23, 2004): 621–27. http://dx.doi.org/10.1083/jcb.200405138.

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Mitochondrial outer and inner membranes contain translocators that achieve protein translocation across and/or insertion into the membranes. Recent evidence has shown that mitochondrial β-barrel protein assembly in the outer membrane requires specific translocator proteins in addition to the components of the general translocator complex in the outer membrane, the TOM40 complex. Here we report two novel mitochondrial outer membrane proteins in yeast, Tom13 and Tom38/Sam35, that mediate assembly of mitochondrial β-barrel proteins, Tom40, and/or porin in the outer membrane. Depletion of Tom13 or Tom38/Sam35 affects assembly pathways of the β-barrel proteins differently, suggesting that they mediate different steps of the complex assembly processes of β-barrel proteins in the outer membrane.

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2

Hancock, R. E. W., R. Siehnel, and N. Martin. "Outer membrane proteins of Pseudomonas." Molecular Microbiology 4, no. 7 (July 1990): 1069–75. http://dx.doi.org/10.1111/j.1365-2958.1990.tb00680.x.

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3

Winter, A. J. "Outer membrane proteins of Brucella." Annales de l'Institut Pasteur / Microbiologie 138, no. 1 (January 1987): 87–89. http://dx.doi.org/10.1016/0769-2609(87)90081-0.

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4

Otzen, Daniel E., and Kell K. Andersen. "Folding of outer membrane proteins." Archives of Biochemistry and Biophysics 531, no. 1-2 (March 2013): 34–43. http://dx.doi.org/10.1016/j.abb.2012.10.008.

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5

Im, Wonpil. "Bacterial Outer Membranes and Interactions with Membrane Proteins." Biophysical Journal 108, no. 2 (January 2015): 370a. http://dx.doi.org/10.1016/j.bpj.2014.11.2030.

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6

Mayer, A., R. Lill, and W. Neupert. "Translocation and insertion of precursor proteins into isolated outer membranes of mitochondria." Journal of Cell Biology 121, no. 6 (June 15, 1993): 1233–43. http://dx.doi.org/10.1083/jcb.121.6.1233.

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Nuclear-encoded proteins destined for mitochondria must cross the outer or both outer and inner membranes to reach their final sub-mitochondrial locations. While the inner membrane can translocate preproteins by itself, it is not known whether the outer membrane also contains an endogenous protein translocation activity which can function independently of the inner membrane. To selectively study the protein transport into and across the outer membrane of Neurospora crassa mitochondria, outer membrane vesicles were isolated which were sealed, in a right-side-out orientation, and virtually free of inner membranes. The vesicles were functional in the insertion and assembly of various outer membrane proteins such as porin, MOM19, and MOM22. Like with intact mitochondria, import into isolated outer membranes was dependent on protease-sensitive surface receptors and led to correct folding and membrane integration. The vesicles were also capable of importing a peripheral component of the inner membrane, cytochrome c heme lyase (CCHL), in a receptor-dependent fashion. Thus, the protein translocation machinery of the outer mitochondrial membrane can function as an independent entity which recognizes, inserts, and translocates mitochondrial preproteins of the outer membrane and the intermembrane space. In contrast, proteins which have to be translocated into or across the inner membrane were only specifically bound to the vesicles, but not imported. This suggests that transport of such proteins involves the participation of components of the intermembrane space and/or the inner membrane, and that in these cases the outer membrane translocation machinery has to act in concert with that of the inner membrane.

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7

Lopez, Job E., William F. Siems, Guy H. Palmer, Kelly A. Brayton, Travis C. McGuire, Junzo Norimine, and Wendy C. Brown. "Identification of Novel Antigenic Proteins in a Complex Anaplasma marginale Outer Membrane Immunogen by Mass Spectrometry and Genomic Mapping." Infection and Immunity 73, no. 12 (December 2005): 8109–18. http://dx.doi.org/10.1128/iai.73.12.8109-8118.2005.

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ABSTRACT Immunization with purified Anaplasma marginale outer membranes induces complete protection against infection that is associated with CD4+ T-lymphocyte-mediated gamma interferon secretion and immunoglobulin G2 (IgG2) antibody titers. However, knowledge of the composition of the outer membrane immunogen is limited. Recent sequencing and annotation of the A. marginale genome predicts at least 62 outer membrane proteins (OMP), enabling a proteomic and genomic approach for identification of novel OMP by use of IgG serum antibody from outer membrane vaccinates. Outer membrane proteins were separated by two-dimensional electrophoresis, and proteins recognized by total IgG and IgG2 in immune sera of outer membrane-vaccinated cattle were detected by immunoblotting. Immunoreactive protein spots were excised and subjected to liquid chromatography-tandem mass spectrometry. A database search of the A. marginale genome identified 24 antigenic proteins that were predicted to be outer membrane, inner membrane, or membrane-associated proteins. These included the previously characterized surface-exposed outer membrane proteins MSP2, operon associated gene 2 (OpAG2), MSP3, and MSP5 as well as recently identified appendage-associated proteins. Among the 21 newly described antigenic proteins, 14 are annotated in the A. marginale genome and include type IV secretion system proteins, elongation factor Tu, and members of the MSP2 superfamily. The identification of these novel antigenic proteins markedly expands current understanding of the composition of the protective immunogen and provides new candidates for vaccine development.

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8

Schwaiger, M., V. Herzog, and W. Neupert. "Characterization of translocation contact sites involved in the import of mitochondrial proteins." Journal of Cell Biology 105, no. 1 (July 1, 1987): 235–46. http://dx.doi.org/10.1083/jcb.105.1.235.

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Import of proteins into the mitochondrial matrix requires translocation across two membranes. Translocational intermediates of mitochondrial proteins, which span the outer and inner membrane simultaneously and thus suggest that translocation occurs in one step, have recently been described (Schleyer, M., and W. Neupert, 1985, Cell, 43:339-350). In this study we present evidence that distinct membrane areas are involved in the translocation process. Mitochondria that had lost most of their outer membrane by digitonin treatment (mitoplasts) still had the ability to import proteins. Import depended on proteinaceous structures of the residual outer membrane and on a factor that is located between the outer and inner membranes and that could be extracted with detergent plus salt. Translocational intermediates, which had been preformed before fractionation, remained with the mitoplasts under conditions where most of the outer membrane was subsequently removed. Submitochondrial vesicles were isolated in which translocational intermediates were enriched. Immunocytochemical studies also suggested that the translocational intermediates are located in areas where outer and inner membranes are in close proximity. We conclude that the membrane-potential-dependent import of precursor proteins involves translocation contact sites where the two membranes are closely apposed and are linked in a stable manner.

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9

Lee, Joonseong, and Wonpil Im. "Modeling and Simulation of Outer Membrane Proteins in Pseudomonas Aeruginosa Outer Membranes." Biophysical Journal 114, no. 3 (February 2018): 241a. http://dx.doi.org/10.1016/j.bpj.2017.11.1344.

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10

Hazlett, Karsten R. O., David L. Cox, Marc Decaffmeyer, Michael P. Bennett, Daniel C. Desrosiers, Carson J. La Vake, Morgan E. La Vake, et al. "TP0453, a Concealed Outer Membrane Protein of Treponema pallidum, Enhances Membrane Permeability." Journal of Bacteriology 187, no. 18 (September 15, 2005): 6499–508. http://dx.doi.org/10.1128/jb.187.18.6499-6508.2005.

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ABSTRACT The outer membrane of Treponema pallidum, the noncultivable agent of venereal syphilis, contains a paucity of protein(s) which has yet to be definitively identified. In contrast, the outer membranes of gram-negative bacteria contain abundant immunogenic membrane-spanning β-barrel proteins mainly involved in nutrient transport. The absence of orthologs of gram-negative porins and outer membrane nutrient-specific transporters in the T. pallidum genome predicts that nutrient transport across the outer membrane must differ fundamentally in T. pallidum and gram-negative bacteria. Here we describe a T. pallidum outer membrane protein (TP0453) that, in contrast to all integral outer membrane proteins of known structure, lacks extensive β-sheet structure and does not traverse the outer membrane to become surface exposed. TP0453 is a lipoprotein with an amphiphilic polypeptide containing multiple membrane-inserting, amphipathic α-helices. Insertion of the recombinant, nonlipidated protein into artificial membranes results in bilayer destabilization and enhanced permeability. Our findings lead us to hypothesize that TP0453 is a novel type of bacterial outer membrane protein which may render the T. pallidum outer membrane permeable to nutrients while remaining inaccessible to antibody.

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11

Tommassen, Jan. "Assembly of outer-membrane proteins in bacteria and mitochondria." Microbiology 156, no. 9 (September 1, 2010): 2587–96. http://dx.doi.org/10.1099/mic.0.042689-0.

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The cell envelope of Gram-negative bacteria consists of two membranes separated by the periplasm. In contrast with most integral membrane proteins, which span the membrane in the form of hydrophobic α-helices, integral outer-membrane proteins (OMPs) form β-barrels. Similar β-barrel proteins are found in the outer membranes of mitochondria and chloroplasts, probably reflecting the endosymbiont origin of these eukaryotic cell organelles. How these β-barrel proteins are assembled into the outer membrane has remained enigmatic for a long time. In recent years, much progress has been reached in this field by the identification of the components of the OMP assembly machinery. The central component of this machinery, called Omp85 or BamA, is an essential and highly conserved bacterial protein that recognizes a signature sequence at the C terminus of its substrate OMPs. A homologue of this protein is also found in mitochondria, where it is required for the assembly of β-barrel proteins into the outer membrane as well. Although accessory components of the machineries are different between bacteria and mitochondria, a mitochondrial β-barrel OMP can be assembled into the bacterial outer membrane and, vice versa, bacterial OMPs expressed in yeast are assembled into the mitochondrial outer membrane. These observations indicate that the basic mechanism of OMP assembly is evolutionarily highly conserved.

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12

Huntley, Jason F., Patrick G. Conley, Kayla E. Hagman, and Michael V. Norgard. "Characterization of Francisella tularensis Outer Membrane Proteins." Journal of Bacteriology 189, no. 2 (November 17, 2006): 561–74. http://dx.doi.org/10.1128/jb.01505-06.

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ABSTRACT Francisella tularensis is a gram-negative coccobacillus that is capable of causing severe, fatal disease in a number of mammalian species, including humans. Little is known about the proteins that are surface exposed on the outer membrane (OM) of F. tularensis, yet identification of such proteins is potentially fundamental to understanding the initial infection process, intracellular survival, virulence, immune evasion and, ultimately, vaccine development. To facilitate the identification of putative F. tularensis outer membrane proteins (OMPs), the genomes of both the type A strain (Schu S4) and type B strain (LVS) were subjected to six bioinformatic analyses for OMP signatures. Compilation of the bioinformatic predictions highlighted 16 putative OMPs, which were cloned and expressed for the generation of polyclonal antisera. Total membranes were extracted from both Schu S4 and LVS by spheroplasting and osmotic lysis, followed by sucrose density gradient centrifugation, which separated OMs from cytoplasmic (inner) membrane and other cellular compartments. Validation of OM separation and enrichment was confirmed by probing sucrose gradient fractions with antibodies to putative OMPs and inner membrane proteins. F. tularensis OMs typically migrated in sucrose gradients between densities of 1.17 and 1.20 g/ml, which differed from densities typically observed for other gram-negative bacteria (1.21 to 1.24 g/ml). Finally, the identities of immunogenic proteins were determined by separation on two-dimensional sodium dodecyl sulfate-polyacrylamide gel electrophoresis and mass spectrometric analysis. This is the first report of a direct method for F. tularensis OM isolation that, in combination with computational predictions, offers a more comprehensive approach for the characterization of F. tularensis OMPs.

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13

Kawahara, M., L. G. Human, K. Kawahara, and G. J. Domingue. "Electroeluted Outer Membrane Proteins as Immunogens." Immunological Investigations 23, no. 3 (January 1994): 223–30. http://dx.doi.org/10.3109/08820139409087802.

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14

Blackall, P. J., D. G. Rogers, and R. Yamamoto. "Outer-Membrane Proteins of Haemophilus paragallinarum." Avian Diseases 34, no. 4 (October 1990): 871. http://dx.doi.org/10.2307/1591376.

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15

Melgosa, Mercedes Perez, Cho-chou Kuo, and Lee Ann Campbell. "Outer membrane complex proteins ofChlamydia pneumoniae." FEMS Microbiology Letters 112, no. 2 (September 1993): 199–204. http://dx.doi.org/10.1111/j.1574-6968.1993.tb06448.x.

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16

JURGENS, U. "Major outer membrane proteins of (Prochloraceae)." FEMS Microbiology Letters 70, no. 2 (July 1990): 125–29. http://dx.doi.org/10.1016/s0378-1097(05)80025-4.

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17

Hatfaludi, Tamás, Keith Al-Hasani, John D. Boyce, and Ben Adler. "Outer membrane proteins of Pasteurella multocida." Veterinary Microbiology 144, no. 1-2 (July 2010): 1–17. http://dx.doi.org/10.1016/j.vetmic.2010.01.027.

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18

Cullen, Paul A., David A. Haake, and Ben Adler. "Outer membrane proteins of pathogenic spirochetes." FEMS Microbiology Reviews 28, no. 3 (June 2004): 291–318. http://dx.doi.org/10.1016/j.femsre.2003.10.004.

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19

Walther, Dirk M., and Doron Rapaport. "Biogenesis of mitochondrial outer membrane proteins." Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1793, no. 1 (January 2009): 42–51. http://dx.doi.org/10.1016/j.bbamcr.2008.04.013.

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20

Puig, Marta, Carme Fusté, and Miquel Viñas. "Outer membrane proteins from Serratia marcescens." Canadian Journal of Microbiology 39, no. 1 (January 1, 1993): 108–11. http://dx.doi.org/10.1139/m93-015.

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The outer membrane proteins (OMPs) of several strains of Serratia marcescens have been studied by sodium dodecyl sulphate – urea – polyacrylamide gel electrophoresis. Four major OMPs, named Omp1, Omp2, Omp3, and OmpA (42, 40, 39, and 37 kDa, respectively), have been visualized. The relative proportions of Omp2 and Omp3 depend on cultural conditions (temperature of incubation, osmolarity, and nutrient availability).Key words: Serratia marcescens, outer membrane proteins, porin.

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21

Zhai, R., F. N. Vögtle, and C. Meisinger. "Degradation of mitochondrial outer membrane proteins." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1817 (October 2012): S162. http://dx.doi.org/10.1016/j.bbabio.2012.06.425.

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22

Slusky, Joanna, and Roland Dunbrack. "Charge Asymmetry in Outer Membrane Proteins." Biophysical Journal 108, no. 2 (January 2015): 240a—241a. http://dx.doi.org/10.1016/j.bpj.2014.11.1331.

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23

Kumar, Amit, Greg Peterson, Tiruvoor G. Nagaraja, and Sanjeev Narayanan. "Outer membrane proteins ofFusobacterium necrophorumsubsp.necrophorumand subsp.funduliforme." Journal of Basic Microbiology 54, no. 8 (May 26, 2013): 812–17. http://dx.doi.org/10.1002/jobm.201200748.

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24

Higgs, Penelope I., Tracy E. Letain, Kelley K. Merriam, Neal S. Burke, HaJeung Park, ChulHee Kang, and Kathleen Postle. "TonB Interacts with Nonreceptor Proteins in the Outer Membrane of Escherichia coli." Journal of Bacteriology 184, no. 6 (March 15, 2002): 1640–48. http://dx.doi.org/10.1128/jb.184.6.1640-1648.2002.

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ABSTRACT The Escherichia coli TonB protein serves to couple the cytoplasmic membrane proton motive force to active transport of iron-siderophore complexes and vitamin B12 across the outer membrane. Consistent with this role, TonB has been demonstrated to participate in strong interactions with both the cytoplasmic and outer membranes. The cytoplasmic membrane determinants for that interaction have been previously characterized in some detail. Here we begin to examine the nature of TonB interactions with the outer membrane. Although the presence of the siderophore enterochelin (also known as enterobactin) greatly enhanced detectable cross-linking between TonB and the outer membrane receptor, FepA, the absence of enterochelin did not prevent the localization of TonB to the outer membrane. Furthermore, the absence of FepA or indeed of all the iron-responsive outer membrane receptors did not alter this association of TonB with the outer membrane. This suggested that TonB interactions with the outer membrane were not limited to the TonB-dependent outer membrane receptors. Hydrolysis of the murein layer with lysozyme did not alter the distribution of TonB, suggesting that peptidoglycan was not responsible for the outer membrane association of TonB. Conversely, the interaction of TonB with the outer membrane was disrupted by the addition of 4 M NaCl, suggesting that these interactions were proteinaceous. Subsequently, two additional contacts of TonB with the outer membrane proteins Lpp and, putatively, OmpA were identified by in vivo cross-linking. These contacts corresponded to the 43-kDa and part of the 77-kDa TonB-specific complexes described previously. Surprisingly, mutations in these proteins individually did not appear to affect TonB phenotypes. These results suggest that there may be multiple redundant sites where TonB can interact with the outer membrane prior to transducing energy to the outer membrane receptors.

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25

Ryan, Kathleen R., James A. Taylor, and Lisa M. Bowers. "The BAM complex subunit BamE (SmpA) is required for membrane integrity, stalk growth and normal levels of outer membrane β-barrel proteins in Caulobacter crescentus." Microbiology 156, no. 3 (March 1, 2010): 742–56. http://dx.doi.org/10.1099/mic.0.035055-0.

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The outer membrane of Gram-negative bacteria is an essential compartment containing a specific complement of lipids and proteins that constitute a protective, selective permeability barrier. Outer membrane β-barrel proteins are assembled into the membrane by the essential hetero-oligomeric BAM complex, which contains the lipoprotein BamE. We have identified a homologue of BamE, encoded by CC1365, which is located in the outer membrane of the stalked alpha-proteobacterium Caulobacter crescentus. BamE associates with proteins whose homologues in other bacteria are known to participate in outer membrane protein assembly: BamA (CC1915), BamB (CC1653) and BamD (CC1984). Caulobacter cells lacking BamE grow slowly in rich medium and are hypersensitive to anionic detergents, some antibiotics and heat exposure, which suggest that the membrane integrity of the mutant is compromised. Membranes of the ΔbamE mutant have normal amounts of the outer membrane protein RsaF, a TolC homologue, but are deficient in CpaC*, an aggregated form of the outer membrane secretin for type IV pili. ΔbamE membranes also contain greatly reduced amounts of three TonB-dependent receptors that are abundant in wild-type cells. Cells lacking BamE have short stalks and are delayed in stalk outgrowth during the cell cycle. Based on these findings, we propose that Caulobacter BamE participates in the assembly of outer membrane β-barrel proteins, including one or more substrates required for the initiation of stalk biogenesis.

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26

Zahedi, Rene P., Albert Sickmann, Andreas M. Boehm, Christiane Winkler, Nicole Zufall, Birgit Schönfisch, Bernard Guiard, Nikolaus Pfanner, and Chris Meisinger. "Proteomic Analysis of the Yeast Mitochondrial Outer Membrane Reveals Accumulation of a Subclass of Preproteins." Molecular Biology of the Cell 17, no. 3 (March 2006): 1436–50. http://dx.doi.org/10.1091/mbc.e05-08-0740.

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Mitochondria consist of four compartments–outer membrane, intermembrane space, inner membrane, and matrix—with crucial but distinct functions for numerous cellular processes. A comprehensive characterization of the proteome of an individual mitochondrial compartment has not been reported so far. We used a eukaryotic model organism, the yeast Saccharomyces cerevisiae, to determine the proteome of highly purified mitochondrial outer membranes. We obtained a coverage of ∼85% based on the known outer membrane proteins. The proteome represents a rich source for the analysis of new functions of the outer membrane, including the yeast homologue (Hfd1/Ymr110c) of the human protein causing Sjögren–Larsson syndrome. Surprisingly, a subclass of proteins known to reside in internal mitochondrial compartments were found in the outer membrane proteome. These seemingly mislocalized proteins included most top scorers of a recent genome-wide analysis for mRNAs that were targeted to mitochondria and coded for proteins of prokaryotic origin. Together with the enrichment of the precursor form of a matrix protein in the outer membrane, we conclude that the mitochondrial outer membrane not only contains resident proteins but also accumulates a conserved subclass of preproteins destined for internal mitochondrial compartments.

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27

Jagannadham, M. V., and S. Saranya. "Analysis of the Membrane proteins of an Antarctic Bacterium Pseudomonas Syringae." Proteomics Insights 4 (January 2011): PRI.S5383. http://dx.doi.org/10.4137/pri.s5383.

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The proteins of an Antarctic bacterium Pseudomonas syringae Lz4W, identified earlier by different membrane protein preparation methods, were combined together and the redundant identities removed. In total, 1479 proteins including 148 outer membrane proteins from this bacterium were predicted by the algorithm PSORTb3.0. A detailed analysis on their subcellular localization was undertaken which was determined using TMHMM, TMB-hunt and BOMP. A comparison of PSORTb predicted outer membrane proteins with BOMP, revealed that most of the proteins predicted by the former, contained β–barrels in the outer membranes. A comparative analysis of PSORTb, TMHMM and TMB-hunt reveals that most of the outer membranes proteins of this bacterium could be identified using this approach. Thus, by using a combination of biochemical and different bioinformatics algorithms, the membrane proteins of P. syringae are analyzed. In particular, PSORTb results are compared and supported by other algorithms, to improve the strength of OM proteins prediction. Several proteins, having an important role in cold adaptation of the organism, could also be identified.

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28

Bowden, G. H., N. Nolette, A. S. McKee, and I. R. Hamilton. "The stability of outer-membrane protein and antigen profiles of a strain of Bacteroides intermedius grown in continuous culture at different pH and growth rates." Canadian Journal of Microbiology 37, no. 5 (May 1, 1991): 368–76. http://dx.doi.org/10.1139/m91-060.

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The stability of the outer-membrane proteins and antigens of a strain of Bacteroides intermedius (VP1 8944 group genotype II) grown in contious culture at varying pH and growth rates (D = 0.025–0.2 h−1, pH 6.0–7.3) has been measured. The membranes showed nine major proteins (> 67–19.55 kilodaltons) and six major antigens (65–28 kilodaltons). Membrane proteins and antigens were stable under the conditions tested; the major proteins were detected in all membranes, and the antigen profiles tested with different antisera showed maximum similarities of 82–95%. Differences did occur in the amounts of membrane proteins synthesized; cells at high growth rates and those growing on the surfaces in the chemostat showed increased amounts of two proteins (40 and 32 kilodaltons) and possibly novel proteins of 24 and 25 kilodaltons. In addition, these membranes reflected increased synthesis or a change to increased reactivity of antigens between 20.5 and 24 kilodaltons. The results indicate stability of the expression of outer-membrane proteins and antigens in environments of differing pH and under different growth rates. However, the amount of these molecules synthesized can vary, and increases in certain proteins and antigens occur as the growth rate increases and the organisms grow on surfaces. Key words: Bacteroides intermedius, outer-membrane antigens, antigenic stability, chemostat culture, outer-membrane profiles.

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29

Bohnert, Maria, Lena-Sophie Wenz, Ralf M. Zerbes, Susanne E. Horvath, David A. Stroud, Karina von der Malsburg, Judith M. Müller, et al. "Role of mitochondrial inner membrane organizing system in protein biogenesis of the mitochondrial outer membrane." Molecular Biology of the Cell 23, no. 20 (October 15, 2012): 3948–56. http://dx.doi.org/10.1091/mbc.e12-04-0295.

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Mitochondria contain two membranes, the outer membrane and the inner membrane with folded cristae. The mitochondrial inner membrane organizing system (MINOS) is a large protein complex required for maintaining inner membrane architecture. MINOS interacts with both preprotein transport machineries of the outer membrane, the translocase of the outer membrane (TOM) and the sorting and assembly machinery (SAM). It is unknown, however, whether MINOS plays a role in the biogenesis of outer membrane proteins. We have dissected the interaction of MINOS with TOM and SAM and report that MINOS binds to both translocases independently. MINOS binds to the SAM complex via the conserved polypeptide transport–associated domain of Sam50. Mitochondria lacking mitofilin, the large core subunit of MINOS, are impaired in the biogenesis of β-barrel proteins of the outer membrane, whereas mutant mitochondria lacking any of the other five MINOS subunits import β-barrel proteins in a manner similar to wild-type mitochondria. We show that mitofilin is required at an early stage of β-barrel biogenesis that includes the initial translocation through the TOM complex. We conclude that MINOS interacts with TOM and SAM independently and that the core subunit mitofilin is involved in biogenesis of outer membrane β-barrel proteins.

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30

Shang, Ellen S., Jonathan T. Skare, Maurice M. Exner, David R. Blanco, Bruce L. Kagan, James N. Miller, and Michael A. Lovett. "Isolation and Characterization of the Outer Membrane ofBorrelia hermsii." Infection and Immunity 66, no. 3 (March 1, 1998): 1082–91. http://dx.doi.org/10.1128/iai.66.3.1082-1091.1998.

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ABSTRACT The outer membrane of Borrelia hermsii has been shown by freeze-fracture analysis to contain a low density of membrane-spanning outer membrane proteins which have not yet been isolated or identified. In this study, we report the purification of outer membrane vesicles (OMV) from B. hermsii HS-1 and the subsequent identification of their constituent outer membrane proteins. The B. hermsii outer membranes were released by vigorous vortexing of whole organisms in low-pH, hypotonic citrate buffer and isolated by isopycnic sucrose gradient centrifugation. The isolated OMV exhibited porin activities ranging from 0.2 to 7.2 nS, consistent with their outer membrane origin. Purified OMV were shown to be relatively free of inner membrane contamination by the absence of measurable β-NADH oxidase activity and the absence of protoplasmic cylinder-associated proteins observed by Coomassie blue staining. Approximately 60 protein spots (some of which are putative isoelectric isomers) with 25 distinct molecular weights were identified as constituents of the OMV enrichment. The majority of these proteins were also shown to be antigenic with sera from B. hermsii-infected mice. Seven of these antigenic proteins were labeled with [3H]palmitate, including the surface-exposed glycerophosphodiester phosphodiesterase, the variable major proteins 7 and 33, and proteins of 15, 17, 38, 42, and 67 kDa, indicating that they are lipoprotein constituents of the outer membrane. In addition, immunoblot analysis of the OMV probed with antiserum to the Borrelia garinii surface-exposed p66/Oms66 porin protein demonstrated the presence of a p66 (Oms66) outer membrane homolog. Treatment of intact B. hermsii with proteinase K resulted in the partial proteolysis of the Oms66/p66 homolog, indicating that it is surface exposed. This identification and characterization of the OMV proteins should aid in further studies of pathogenesis and immunity of tick-borne relapsing fever.

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31

Yu, Hong, Karuna P. Karunakaran, Xiaozhou Jiang, Queenie Chan, Caren Rose, Leonard J. Foster, Raymond M. Johnson, and Robert C. Brunham. "Comparison of Chlamydia outer membrane complex to recombinant outer membrane proteins as vaccine." Vaccine 38, no. 16 (April 2020): 3280–91. http://dx.doi.org/10.1016/j.vaccine.2020.02.059.

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32

Braun, Volkmar, and Franziska Endriß. "Energy-coupled outer membrane transport proteins and regulatory proteins." BioMetals 20, no. 3-4 (March 17, 2007): 219–31. http://dx.doi.org/10.1007/s10534-006-9072-5.

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33

Braun, Volkmar. "The Outer Membrane Took Center Stage." Annual Review of Microbiology 72, no. 1 (September 8, 2018): 1–24. http://dx.doi.org/10.1146/annurev-micro-090817-062156.

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My interest in membranes was piqued during a lecture series given by one of the founders of molecular biology, Max Delbrück, at Caltech, where I spent a postdoctoral year to learn more about protein chemistry. That general interest was further refined to my ultimate research focal point—the outer membrane of Escherichia coli—through the influence of the work of Wolfhard Weidel, who discovered the murein (peptidoglycan) layer and biochemically characterized the first phage receptors of this bacterium. The discovery of lipoprotein bound to murein was completely unexpected and demonstrated that the protein composition of the outer membrane and the structure and function of proteins could be unraveled at a time when nothing was known about outer membrane proteins. The research of my laboratory over the years covered energy-dependent import of proteinaceous toxins and iron chelates across the outer membrane, which does not contain an energy source, and gene regulation by iron, including transmembrane transcriptional regulation.

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Pon, L., T. Moll, D. Vestweber, B. Marshallsay, and G. Schatz. "Protein import into mitochondria: ATP-dependent protein translocation activity in a submitochondrial fraction enriched in membrane contact sites and specific proteins." Journal of Cell Biology 109, no. 6 (December 1, 1989): 2603–16. http://dx.doi.org/10.1083/jcb.109.6.2603.

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To identify the membrane regions through which yeast mitochondria import proteins from the cytoplasm, we have tagged these regions with two different partly translocated precursor proteins. One of these was bound to the mitochondrial surface of ATP-depleted mitochondria and could subsequently be chased into mitochondria upon addition of ATP. The other intermediate was irreversibly stuck across both mitochondrial membranes at protein import sites. Upon subfraction of the mitochondria, both intermediates cofractionated with membrane vesicles whose buoyant density was between that of inner and outer membranes. When these vesicles were prepared from mitochondria containing the chaseable intermediate, they internalized it upon addition of ATP. A non-hydrolyzable ATP analogue was inactive. This vesicle fraction contained closed, right-side-out inner membrane vesicles attached to leaky outer membrane vesicles. The vesicles contained the mitochondrial binding sites for cytoplasmic ribosomes and contained several mitochondrial proteins that were enriched relative to markers of inner or outer membranes. By immunoelectron microscopy, two of these proteins were concentrated at sites where mitochondrial inner and outer membranes are closely apposed. We conclude that these vesicles contain contact sites between the two mitochondrial membranes, that these sites are the entry point for proteins into mitochondria, and that the isolated vesicles are still translocation competent.

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Becker, Thomas, Lena-Sophie Wenz, Vivien Krüger, Waltraut Lehmann, Judith M. Müller, Luise Goroncy, Nicole Zufall, et al. "The mitochondrial import protein Mim1 promotes biogenesis of multispanning outer membrane proteins." Journal of Cell Biology 194, no. 3 (August 8, 2011): 387–95. http://dx.doi.org/10.1083/jcb.201102044.

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The mitochondrial outer membrane contains translocase complexes for the import of precursor proteins. The translocase of the outer membrane complex functions as a general preprotein entry gate, whereas the sorting and assembly machinery complex mediates membrane insertion of β-barrel proteins of the outer membrane. Several α-helical outer membrane proteins are known to carry multiple transmembrane segments; however, only limited information is available on the biogenesis of these proteins. We report that mitochondria lacking the mitochondrial import protein 1 (Mim1) are impaired in the biogenesis of multispanning outer membrane proteins, whereas overexpression of Mim1 stimulates their import. The Mim1 complex cooperates with the receptor Tom70 in binding of precursor proteins and promotes their insertion and assembly into the outer membrane. We conclude that the Mim1 complex plays a central role in the import of α-helical outer membrane proteins with multiple transmembrane segments.

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Murcha, Monika W., Dina Elhafez, A. Harvey Millar, and James Whelan. "The C-terminal Region of TIM17 Links the Outer and Inner Mitochondrial Membranes inArabidopsisand Is Essential for Protein Import." Journal of Biological Chemistry 280, no. 16 (February 18, 2005): 16476–83. http://dx.doi.org/10.1074/jbc.m413299200.

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The translocase of the inner membrane 17 (AtTIM17-2) protein fromArabidopsishas been shown to link the outer and inner mitochondrial membranes. This was demonstrated by several approaches: (i)In vitroorganelle import assays indicated the importedAtTIM17-2 protein remained protease accessible in the outer membrane when inserted into the inner membrane. (ii) N-terminal and C-terminal tagging indicated that it was the C-terminal region that was located in the outer membrane. (iii) Antibodies raised to the C-terminal 100 amino acids recognize a 31-kDa protein from purified mitochondria, but cross-reactivity was abolished when mitochondria were protease-treated to remove outer membrane-exposed proteins. Antibodies toAtTIM17-2 inhibited import of proteins via the general import pathway into outer membrane-ruptured mitochondria, but did not inhibit protein import via the carrier import pathway. Together these results indicate that the C-terminal region ofAtTIM17-2 is exposed on the outer surface of the outer membrane, and the C-terminal region is essential for protein import into mitochondria.

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Hoffmann, Juliane J., and Thomas Becker. "Crosstalk between Mitochondrial Protein Import and Lipids." International Journal of Molecular Sciences 23, no. 9 (May 9, 2022): 5274. http://dx.doi.org/10.3390/ijms23095274.

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Mitochondria import about 1000 precursor proteins from the cytosol. The translocase of the outer membrane (TOM complex) forms the major entry site for precursor proteins. Subsequently, membrane-bound protein translocases sort the precursor proteins into the outer and inner membrane, the intermembrane space, and the matrix. The phospholipid composition of mitochondrial membranes is critical for protein import. Structural and biochemical data revealed that phospholipids affect the stability and activity of mitochondrial protein translocases. Integration of proteins into the target membrane involves rearrangement of phospholipids and distortion of the lipid bilayer. Phospholipids are present in the interface between subunits of protein translocases and affect the dynamic coupling of partner proteins. Phospholipids are required for full activity of the respiratory chain to generate membrane potential, which in turn drives protein import across and into the inner membrane. Finally, outer membrane protein translocases are closely linked to organellar contact sites that mediate lipid trafficking. Altogether, intensive crosstalk between mitochondrial protein import and lipid biogenesis controls mitochondrial biogenesis.

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Chenoweth, Matthew R., Craig E. Greene, Duncan C. Krause, and Frank C. Gherardini. "Predominant Outer Membrane Antigens of Bartonella henselae." Infection and Immunity 72, no. 6 (June 2004): 3097–105. http://dx.doi.org/10.1128/iai.72.6.3097-3105.2004.

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ABSTRACT A hallmark of Bartonella henselae is persistent bacteremia in cats despite the presence of a vigorous host immune response. To understand better the long-term survival of B. henselae in cats, we examined the feline humoral immune response to B. henselae outer membrane (OM) proteins in naturally and experimentally infected cats. Initially, a panel of sera (n = 42) collected throughout North America from naturally infected cats was used to probe B. henselae total membranes to detect commonly recognized antigens. Twelve antigens reacted with sera from at least 85% of cats, and five were recognized by sera from all cats. To localize these antigens further, OMs were purified on discontinuous sucrose density step gradients. Each membrane fraction (OM, hybrid or inner membrane [IM]) contained less than 1% of the total malate dehydrogenase activity (soluble marker), indicating very little contamination by cytoplasmic proteins. FtsI, an integral IM cell division protein, was used to identify the low-density fraction (ρ = 1.13 g/cm3) as putative IM (<5% of the total FtsI localized to the high-density fraction) while lipopolysaccharide (LPS) and Pap31, a homolog of the Bartonella quintana heme-binding protein A (HbpA), defined the high-density fraction (ρ = 1.20 g/cm3) as putative OM. Additionally, little evidence of cross-contamination between the IM and OM was evident by two-dimensional gel electrophoresis. When purified OMs were probed with feline sera, antigenic proteins profiles were very similar to those observed with total membranes, indicating that many, but not all, of the immunoreactive proteins detected in the initial immunoblots were OM components. Interestingly, two-dimensional immunoblots indicated that B. henselae LPS and members of the Hbp family of proteins did not appear to stimulate an humoral response in any infected cats. Seven proteins were recognized by at least 70% of sera tested, but only three were recognized by all sera. Nanospray-tandem mass spectrometry was used to identify OM components, including the immunodominant OM proteins. Recognition of the nonimmunogenic nature of the major OM components, such as LPS, and identification of the predominant immunogens should elucidate the mechanisms by which B. henselae establishes persistent bacteremic infections within cats. Additionally, the common antigens may serve as potential feline vaccine candidates to eliminate the pathogen from its animal reservoir.

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Ellenrieder, Lars, Christoph U. Mårtensson, and Thomas Becker. "Biogenesis of mitochondrial outer membrane proteins, problems and diseases." Biological Chemistry 396, no. 11 (November 1, 2015): 1199–213. http://dx.doi.org/10.1515/hsz-2015-0170.

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Abstract Proteins of the mitochondrial outer membrane are synthesized as precursors on cytosolic ribosomes and sorted via internal targeting sequences to mitochondria. Two different types of integral outer membrane proteins exist: proteins with a transmembrane β-barrel and proteins embedded by a single or multiple α-helices. The import pathways of these two types of membrane proteins differ fundamentally. Precursors of β-barrel proteins are first imported across the outer membrane via the translocase of the outer membrane (TOM complex). The TOM complex is coupled to the sorting and assembly machinery (SAM complex), which catalyzes folding and membrane insertion of these precursors. The mitochondrial import machinery (MIM complex) promotes import of proteins with multiple α-helical membrane spans. Depending on the topology precursors of proteins with a single α-helical membrane anchor are imported via several distinct routes. We summarize current models and open questions of biogenesis of mitochondrial outer membrane proteins and discuss the impact of malfunctions of protein sorting on the development of diseases.

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Bédard, Jocelyn, and Paul Jarvis. "Green light for chloroplast outer-membrane proteins." Nature Cell Biology 10, no. 2 (February 2008): 120–22. http://dx.doi.org/10.1038/ncb0208-120.

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Owen, Peter, Mary Meehan, Helen de Loughry-Doherty, and Ian Henderson. "Phase-variable outer membrane proteins inEscherichia coli." FEMS Immunology & Medical Microbiology 16, no. 2 (December 1996): 63–76. http://dx.doi.org/10.1111/j.1574-695x.1996.tb00124.x.

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Passerini de Rossi, Beatriz N., Laura E. Friedman, F. Luis GonzÃ¡lez Flecha, Pablo R. Castello, Mirta A. Franco, and Juan Pablo F. C. Rossi. "Identification ofBordetella pertussisvirulence-associated outer membrane proteins." FEMS Microbiology Letters 172, no. 1 (March 1999): 9–13. http://dx.doi.org/10.1111/j.1574-6968.1999.tb13442.x.

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Bakken, V., and H. B. Jensen. "Outer Membrane Proteins of Fusobacterium nucleatum Fev1." Microbiology 132, no. 4 (April 1, 1986): 1069–78. http://dx.doi.org/10.1099/00221287-132-4-1069.

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Lång, Hannu. "Outer membrane proteins as surface display systems." International Journal of Medical Microbiology 290, no. 7 (December 2000): 579–85. http://dx.doi.org/10.1016/s1438-4221(00)80004-1.

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Veiga-Crespo, P., E. Fusté, T. Vinuesa, M. Viñas, and T. G. Villa. "Synergism between Outer Membrane Proteins and Antimicrobials." Antimicrobial Agents and Chemotherapy 55, no. 5 (February 14, 2011): 2206–11. http://dx.doi.org/10.1128/aac.01786-10.

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ABSTRACTAntibiotic-resistant bacteria are becoming one of the most important problems in health care because of the number of resistant strains and the paucity of new effective antimicrobials. Since antibiotic-resistant bacteria will continue to increase, it is necessary to look for new alternative strategies to fight against them. It is generally accepted that Gram-negative bacteria are intrinsically less susceptible than Gram-positive bacteria to antimicrobials. The main reason is that Gram-negative bacteria are surrounded by a permeability barrier known as the outer membrane (OM). Hydrophilic solutes most often cross the OM through water-filled channels formed by a particular family of proteins known as porins. This work explores the possibility of using exogenous porins to lower the required amounts of antibiotics (ampicillin, ciprofloxacin, cefotaxime, clindamycin, erythromycin, and tetracycline). Porins had a bactericidal effect onEscherichia colicultures, mainly in the logarithmic phase of growth, when combined with low antibiotic concentrations. The use of different antibiotic-porin mixtures showed a bactericidal effect greater than those of antibiotics and porins when used separately. It was possible to observe different behaviors according to the antibiotic type used.

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BRZOSTEK, K., and W. NICHOLS. "Outer membrane permeability and porin proteins of." FEMS Microbiology Letters 70, no. 3 (August 1990): 275–77. http://dx.doi.org/10.1016/s0378-1097(05)80007-2.

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Schulz, Georg E. "The structure of bacterial outer membrane proteins." Biochimica et Biophysica Acta (BBA) - Biomembranes 1565, no. 2 (October 2002): 308–17. http://dx.doi.org/10.1016/s0005-2736(02)00577-1.

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Fjellbirkeland, A., Hans Kleivdal, Carsten Joergensen, Helle Thestrup, and Harald B. Jensen. "Outer membrane proteins of Methylococcus capsulatus (Bath)." Archives of Microbiology 168, no. 2 (August 5, 1997): 128–35. http://dx.doi.org/10.1007/s002030050478.

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Becker, T., L. S. Wenz, and N. Pfanner. "Biogenesis of alpha-helical outer membrane proteins." Biochimica et Biophysica Acta (BBA) - Bioenergetics 1817 (October 2012): S67—S68. http://dx.doi.org/10.1016/j.bbabio.2012.06.191.

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Beis, Konstantinos, Chris Whitfield, Ian Booth, and James H. Naismith. "Two-step purification of outer membrane proteins." International Journal of Biological Macromolecules 39, no. 1-3 (August 2006): 10–14. http://dx.doi.org/10.1016/j.ijbiomac.2005.12.008.

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