The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
PROTEASES AND THEIR TARGETS IN ESCHERICHIA COLI
Abstract
▪ Abstract Proteolysis in Escherichia coli serves to rid the cell of abnormal and misfolded proteins and to limit the time and amounts of availability of critical regulatory proteins. Most intracellular proteolysis is initiated by energy-dependent proteases, including Lon, ClpXP, and HflB; HflB is the only essential E. coli protease. The ATPase domains of these proteases mediate substrate recognition. Recognition elements in target are not well defined, but are probably not specific amino acid sequences. Naturally unstable protein substrates include the regulatory sigma factors for heat shock and stationary phase gene expression, σ32 and RpoS. Other cellular proteins serve as environmental sensors that modulate the availability of the unstable proteins to the proteases, resulting in rapid changes in sigma factor levels and therefore in gene transcription. Many of the specific proteases found in E. coli are well-conserved in both prokaryotes and eukaryotes, and serve critical functions in developmental systems.
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Citations
Cites
Role of a peptide tagging system in degradation of proteins synthesized from damaged messenger RNA
Keiler, K. C., Waller, P. R. H., & Sauer, R. T. (1996) · Science · doi:10.1126/science.271.5251.990 · Cited by 1,125
An inducible DNA replication–cell division coupling mechanism in E. coli
Huisman, O., & D'Ari, R. (1981) · Nature · doi:10.1038/290797a0 · Cited by 451
Cited by
Recombinant protein expression in Escherichia coli: advances and challenges
Rosano, G. L., & Ceccarelli, E. A. (2014) · Frontiers in Microbiology · doi:10.3389/fmicb.2014.00172 · Cited by 2,556
The 26S Proteasome: A Molecular Machine Designed for Controlled Proteolysis
Voges, D., Zwickl, P., & Baumeister, W. (1999) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.68.1.1015 · Cited by 1,608
Principles of genetic circuit design
Brophy, J. A. N., & Voigt, C. A. (2014) · Nature Methods · doi:10.1038/nmeth.2926 · Cited by 931
Gottesman, S., Roche, E., Zhou, Y., & Sauer, R. T. (1998) · Genes & Development · doi:10.1101/gad.12.9.1338 · Cited by 835
Self-citationA Temperature-Dependent Switch from Chaperone to Protease in a Widely Conserved Heat Shock Protein
Spiess, C., Beil, A., & Ehrmann, M. (1999) · Cell · doi:10.1016/s0092-8674(00)80743-6 · Cited by 768
Metadata
- Authors
- Gottesman, S.
- Venue
- Annual Review of Genetics
- Publisher
- Annual Reviews
- Published
- 1996-12
- Volume
- 30
- Issue
- 1
- Pages
- 465-506
- ISSN
- 0066-4197 (ISSN-L)
- 1545-2948
- OpenAlex
- W2099196052
- Cited by
- 717
- References
- 2
- FWCI
- 2.34
- Type
- journal article
- Language
- en
- Open access
- closed
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- Gottesman, S. (1996). PROTEASES AND THEIR TARGETS IN ESCHERICHIA COLI. Annual Review of Genetics. https://doi.org/10.1146/annurev.genet.30.1.465
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
