The DOI matches its Crossref record; 114 of the 114 references it cites were found in a registry or an index.
Proteolysis in Bacterial Regulatory Circuits
Abstract
▪ Abstract Proteolysis by cytoplasmic, energy-dependent proteases plays a critical role in many regulatory circuits, keeping basal levels of regulatory proteins low and rapidly removing proteins when they are no longer needed. In bacteria, four families of energy-dependent proteases carry out degradation. In all of them, substrates are first recognized and bound by ATPase domains and then unfolded and translocated to a sequestered proteolytic chamber. Substrate selection depends not on ubiquitin but on intrinsic recognition signals within the proteins and, in some cases, on adaptor or effector proteins that participate in delivering the substrate to the protease. For some, the activity of these adaptors can be regulated, which results in regulated proteolysis. Recognition motifs for proteolysis are frequently found at the N and C termini of substrates. Proteolytic switches appear to be critical for cell cycle development in Caulobacter crescentus, for proper sporulation in Bacillus subtilis, and for the transition in and out of stationary phase in Escherichia coli. In eukaryotes, the same proteases are found in organelles, where they also play important roles.
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ClpP Mediates Activation of a Mitochondrial Unfolded Protein Response in C. elegans
Haynes, C. M., Petrova, K., Benedetti, C., Yang, Y., & Ron, D. (2007) · Developmental Cell · doi:10.1016/j.devcel.2007.07.016 · Cited by 592
Sculpting the Proteome with AAA+ Proteases and Disassembly Machines
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AphA and LuxR/HapR reciprocally control quorum sensing in vibrios
Rutherford, S. T., van Kessel, J. C., Shao, Y., & Bassler, B. L. (2011) · Genes & Development · doi:10.1101/gad.2015011 · Cited by 293
Frees, D., Savijoki, K., Varmanen, P., & Ingmer, H. (2007) · Molecular Microbiology · doi:10.1111/j.1365-2958.2007.05598.x · Cited by 288
Metadata
- Authors
- Gottesman, S.
- Venue
- Annual Review of Cell and Developmental Biology
- Publisher
- Annual Reviews
- Published
- 2003-11
- Volume
- 19
- Issue
- 1
- Pages
- 565-587
- ISSN
- 1081-0706 (ISSN-L)
- 1530-8995
- OpenAlex
- W2119349093
- Cited by
- 422
- References
- 114
- FWCI
- 1.51
- Type
- journal article
- Language
- en
- Open access
- closed
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