The DOI matches its Crossref record; 43 of the 43 references it cites were found in a registry or an index.
Assembly Factor Omp85 Recognizes Its Outer Membrane Protein Substrates by a Species-Specific C-Terminal Motif
Open accessAbstract
Integral beta-barrel proteins are found in the outer membranes of Gram-negative bacteria, mitochondria, and chloroplasts. The assembly of these proteins requires a proteinaceous apparatus of which Omp85 is an evolutionary conserved central component. To study its molecular mechanism, we have produced Omp85 from Escherichia coli in inclusion bodies and refolded it in vitro. The interaction of Omp85 with its substrate proteins was studied in lipid-bilayer experiments, where it formed channels. The properties of these channels were affected upon addition of unfolded outer-membrane proteins (OMPs) or synthetic peptides corresponding to their C-terminal signature sequences. The interaction exhibited species specificity, explaining the inefficient assembly of OMPs from Neisseria in E. coli. Accordingly, the in vivo assembly of the neisserial porin PorA into the E. coli outer membrane was accomplished after adapting its signature sequence. These results demonstrate that the Omp85 assembly machinery recognizes OMPs by virtue of their C-terminal signature sequence.
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Cites
Crystal structures explain functional properties of two E. coli porins
Cowan, S. W., Schirmer, T., Rummel, G., Steiert, M., Ghosh, R., Pauptit, R. A., Jansonius, J. N., & Rosenbusch, J. P. (1992) · Nature · doi:10.1038/358727a0 · Cited by 1,520
Lugtenberg, B., Meijers, J., Peters, R., van der Hoek, P., & van Alphen, L. (1975) · FEBS Letters · doi:10.1016/0014-5793(75)80272-9 · Cited by 1,416
Structure and function of bacterial outer membrane proteins: barrels in a nutshell
Koebnik, R., Locher, K. P., & Van Gelder, P. (2000) · Molecular Microbiology · doi:10.1046/j.1365-2958.2000.01983.x · Cited by 1,202
Wu, T., Malinverni, J., Ruiz, N., Kim, S., Silhavy, T. J., & Kahne, D. (2005) · Cell · doi:10.1016/j.cell.2005.02.015 · Cited by 769
Role of a Highly Conserved Bacterial Protein in Outer Membrane Protein Assembly
Voulhoux, R., Bos, M. P., Geurtsen, J., Mols, M., & Tommassen, J. (2003) · Science · doi:10.1126/science.1078973 · Cited by 742
Self-citationWalsh, N. P., Alba, B. M., Bose, B., Gross, C. A., & Sauer, R. T. (2003) · Cell · doi:10.1016/s0092-8674(03)00203-4 · Cited by 508
Struyvé, M., Moons, M., & Tommassen, J. (1991) · Journal of Molecular Biology · doi:10.1016/0022-2836(91)90880-f · Cited by 485
Self-citationEvolutionary conservation of biogenesis of β-barrel membrane proteins
Paschen, S. A., Waizenegger, T., Stan, T., Preuss, M., Cyrklaff, M., Hell, K., Rapaport, D., & Neupert, W. (2003) · Nature · doi:10.1038/nature02208 · Cited by 431
PROTEIN TRANSLOCATION BY THE SEC61/SECY CHANNEL
Osborne, A. R., Rapoport, T. A., & van den Berg, B. (2005) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.21.012704.133214 · Cited by 391
The Omp85 family of proteins is essential for outer membrane biogenesis in mitochondria and bacteria
Gentle, I., Gabriel, K., Beech, P., Waller, R., & Lithgow, T. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200310092 · Cited by 373
Cited by
Type V secretion: mechanism(s) of autotransport through the bacterial outer membrane
Leo, J. C., Grin, I., & Linke, D. (2012) · Philosophical Transactions of the Royal Society B Biological Sciences · doi:10.1098/rstb.2011.0208 · Cited by 269
General features of transmembrane beta barrels from a large database
Montezano, D., Bernstein, R., Copeland, M. M., & Slusky, J. S. G. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2220762120 · Cited by 17
Metadata
- Authors
- Robert, V., Volokhina, E. B., Senf, F., Bos, M. P., Gelder, P. V., & Tommassen, J.
- Venue
- PLoS Biology
- Publisher
- Public Library of Science (PLoS)
- Published
- 2006-11-07
- Volume
- 4
- Issue
- 11
- Pages
- e377
- ISSN
- 1544-9173 (ISSN-L)
- 1545-7885
- OpenAlex
- W2053754839
- Cited by
- 326
- References
- 43
- FWCI
- 11.31
- Type
- journal article
- Language
- en
- Open access
- gold
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- Robert, V., Volokhina, E. B., Senf, F., Bos, M. P., Gelder, P. V., & Tommassen, J. (2006). Assembly Factor Omp85 Recognizes Its Outer Membrane Protein Substrates by a Species-Specific C-Terminal Motif. PLoS Biology. https://doi.org/10.1371/journal.pbio.0040377
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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