Cited by 332Bacterial Genetics and BiotechnologyRNA and protein synthesis mechanismsHeat shock proteins research

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The E. coli signal recognition particle is required for the insertion of a subset of inner membrane proteins.

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Ulbrandt, Nancy D, Newitt, John A, Bernstein, Harris D·1997·Cell

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Abstract

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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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
The physical map of the whole E. coli chromosome: Application of a new strategy for rapid analysis and sorting of a large genomic library
Kohara, Y., Akiyama, K., & Isono, K. (1987) · Cell · doi:10.1016/0092-8674(87)90503-4 · Cited by 1,754
Cloning and stable maintenance of 300-kilobase-pair fragments of human DNA in Escherichia coli using an F-factor-based vector.
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
A subfamily of stress proteins facilitates translocation of secretory and mitochondrial precursor polypeptides
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

Show all 49 references

Research works printed but not linked: 1

Claros, 1994, TopPred II, Comput. Appl. Biosci., 10, 685

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Bibi, E. (1998) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(97)01134-1 · Cited by 42
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Self-citation
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Structure of the most conserved internal loop in SRP RNA.
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Authors: Ulbrandt, N. D., Newitt, J. A., & Bernstein, H. D.
Affiliations: National Institutes of Health (US)
Corresponding author: Newitt, John A
Bernstein, Harris D
ORCID: Ulbrandt, Nancy D
Newitt, John A
Venue: Cell
Publisher: Elsevier BV
Published: 1997-01
Volume: 88
Issue: 2
Pages: 187-196
ISSN: 0092-8674 (ISSN-L)
DOI: 10.1016/s0092-8674(00)81839-5
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: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 6041 d)
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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The E. coli signal recognition particle is required for the insertion of a subset of inner membrane proteins.

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