The DOI matches its Crossref record; 32 of the 32 references it cites were found in a registry or an index.
Overlapping recognition determinants within the ssrA degradation tag allow modulation of proteolysis
Open accessAbstract
The ssrA tag, an 11-aa peptide added to the C terminus of proteins stalled during translation, targets proteins for degradation by ClpXP and ClpAP. Mutational analysis of the ssrA tag reveals independent, but overlapping determinants for its interactions with ClpX, ClpA, and SspB, a specificity-enhancing factor for ClpX. ClpX interacts with residues 9–11 at the C terminus of the tag, whereas ClpA recognizes positions 8–10 in addition to residues 1–2 at the N terminus. SspB interacts with residues 1–4 and 7, N-terminal to the ClpX-binding determinants, but overlapping the ClpA determinants. As a result, SspB and ClpX work together to recognize ssrA-tagged substrates efficiently, whereas SspB inhibits recognition of these substrates by ClpA. Thus, dissection of the recognition signals within the ssrA tag provides insight into how multiple proteins function in concert to modulate proteolysis.
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Cites
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Self-citationThe Structure of ClpP at 2.3 Å Resolution Suggests a Model for ATP-Dependent Proteolysis
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Cited by
Sculpting the Proteome with AAA+ Proteases and Disassembly Machines
Sauer, R. T., Bolon, D. N., Burton, B. M., Burton, R. E., Flynn, J. M., Grant, R. A., Hersch, G. L., Joshi, S. A., Kenniston, J. A., Levchenko, I., et al. (2004) · Cell · doi:10.1016/j.cell.2004.09.020 · Cited by 462
Self-citationBittner, L.-M., Westphal, K., & Narberhaus, F. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.648550 · Cited by 34
Harnessing Machine Learning To Unravel Protein Degradation in Escherichia coli
Nagar, N., Ecker, N., Loewenthal, G., Avram, O., Ben-Meir, D., Biran, D., Ron, E., & Pupko, T. (2021) · mSystems · doi:10.1128/msystems.01296-20 · Cited by 31
Orthogonal Degron System for Controlled Protein Degradation in Cyanobacteria
Sakkos, J. K., Hernandez-Ortiz, S., Osteryoung, K. W., & Ducat, D. C. (2021) · ACS Synthetic Biology · doi:10.1021/acssynbio.1c00035 · Cited by 21
Filament formation activates protease and ring nuclease activities of CRISPR Lon-SAVED
Smalakyte, D., Ruksenaite, A., Sasnauskas, G., Tamulaitiene, G., & Tamulaitis, G. (2024) · Molecular Cell · doi:10.1016/j.molcel.2024.09.002 · Cited by 17
Metadata
- Authors
- Flynn, J. M., Levchenko, I., Seidel, M., Wickner, S. H., Sauer, R. T., & Baker, T. A.
- Venue
- Proceedings of the National Academy of Sciences
- Published
- 2001-09-04
- Volume
- 98
- Issue
- 19
- Pages
- 10584-10589
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- OpenAlex
- W2099102896
- Cited by
- 334
- References
- 32
- FWCI
- 5.43
- Type
- journal article
- Language
- en
- Open access
- green
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