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The E. coli signal recognition particle is required for the insertion of a subset of inner membrane proteins.
Open accessAbstract
E. coli homologs of the signal recognition particle (SRP) and its receptor are essential for viability, but their role in protein export is unclear. To elucidate their function, we devised a genome-wide screen to identify genes that encode SRP substrates. Inhibition of the SRP pathway sharply blocked the membrane insertion of several polytopic inner membrane proteins (IMPs) that were predicted to be SRP substrates, but had a smaller effect on the insertion of other IMPs and no significant effect on preprotein translocation. Our results suggest that whereas most E. coli preproteins and some IMPs can utilize SRP-independent targeting pathways effectively, the structural features of a subset of IMPs have required the conservation of an SRP-based targeting machinery.
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“The SRP pathway is a universally conserved targeting system that bacteria primarily use for inner membrane proteins”
From The Dynamic SecYEG Translocon (2021) · cites this paper as Ulbrandt et al., 1997
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Altschul, S. F., Gish, W., Miller, W., Myers, E. W., & Lipman, D. J. (1990) · Journal of Molecular Biology · doi:10.1006/jmbi.1990.9999 · Cited by 98,669
Antibodies, a laboratory manual
(1989) · Biomedicine & Pharmacotherapy · doi:10.1016/0753-3322(89)90130-3 · Cited by 12,318
A short course in bacterial genetics
Miller, J. H. (1992) · Cited by 4,391
The GTPase superfamily: conserved structure and molecular mechanism
Bourne, H. R., Sanders, D. A., & McCormick, F. (1991) · Nature · doi:10.1038/349117a0 · Cited by 3,392
Kohara, Y., Akiyama, K., & Isono, K. (1987) · Cell · doi:10.1016/0092-8674(87)90503-4 · Cited by 1,754
Shizuya, H., Birren, B. W., Kim, U. J., Mancino, V., Slepak, T. I., Tachiiri, Y., & Simon, M. I. (1992) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.89.18.8794 · Cited by 1,672
Escherichia coli and Salmonella.
Neidhart, F. C. (1996) · Cited by 1,577
Deshaies, R., Koch, B., Werner-Washburne, M., Craig, E., & Schekman, R. (1988) · Nature · doi:10.1038/332800a0 · Cited by 1,368
70K heat shock related proteins stimulate protein translocation into microsomes
Chirico, W. J., Waters, M. G., & Blobel, G. (1988) · Nature · doi:10.1038/332805a0 · Cited by 1,232
Common Principles of Protein Translocation Across Membranes
Schatz, G., & Dobberstein, B. (1996) · Science · doi:10.1126/science.271.5255.1519 · Cited by 1,116
Research works printed but not linked: 1
- Claros, 1994, TopPred II, Comput. Appl. Biosci., 10, 685
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Metadata
- Authors
- Ulbrandt, N. D., Newitt, J. A., & Bernstein, H. D.
- Affiliations
- National Institutes of Health (US)
- Corresponding author
- Newitt, John A
- Bernstein, Harris D
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 1997-01
- Volume
- 88
- Issue
- 2
- Pages
- 187-196
- ISSN
- 0092-8674 (ISSN-L)
- OpenAlex
- W2000023769
- Cited by
- 332
- References
- 49
- Citations by year
- 2026: 1 · 2025: 2 · 2024: 1 · 2023: 1 · 2022: 4 · 2021: 7 · 2020: 4 · 2019: 6 · 2018: 5 · 2017: 9 · 2016: 7 · 2015: 2 · 2014: 8 · 2013: 13 · 2012: 9
- FWCI
- 19.14
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Bacterial Genetics and Biotechnology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Heat shock proteins research
- Keywords
- signal recognition particle, SRP receptor, polytopic membrane proteins, protein targeting, genome-wide screen, preprotein translocation, Escherichia coli
- MeSH terms
- Bacterial Proteins, Biological Transport, Escherichia coli, Genes, Bacterial, Membrane Proteins, Phenotype, Protein Precursors, Recombinant Fusion Proteins, Transformation, Bacterial, Mutagenesis, Site-Directed, Receptors, Cytoplasmic and Nuclear, Signal Recognition Particle, Escherichia coli Proteins
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