The DOI matches its Crossref record; 16 of the 16 references it cites were found in a registry or an index.
A Specificity-Enhancing Factor for the ClpXP Degradation Machine
Abstract
Events that stall bacterial protein synthesis activate the ssrA-tagging machinery, resulting in resumption of translation and addition of an 11-residue peptide to the carboxyl terminus of the nascent chain. This ssrA-encoded peptide tag marks the incomplete protein for degradation by the energy-dependent ClpXP protease. Here, a ribosome-associated protein, SspB, was found to bind specifically to ssrA-tagged proteins and to enhance recognition of these proteins by ClpXP. Cells with an sspB mutation are defective in degrading ssrA-tagged proteins, demonstrating that SspB is a specificity-enhancing factor for ClpXP that controls substrate choice.
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Self-citationHSP100/Clp proteins: a common mechanism explains diverse functions
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The structures of HslU and the ATP-dependent protease HslU–HslV
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The SsrA–SmpB system for protein tagging, directed degradation and ribosome rescue
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Self-citationGlobal unfolding of a substrate protein by the Hsp100 chaperone ClpA
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Dynamics of Substrate Denaturation and Translocation by the ClpXP Degradation Machine
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Sculpting the Proteome with AAA+ Proteases and Disassembly Machines
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Self-citationAn unstructured initiation site is required for efficient proteasome-mediated degradation
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Proteolysis in Bacterial Regulatory Circuits
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Metadata
- Authors
- Levchenko, I., Seidel, M., Sauer, R. T., & Baker, T. A.
- Venue
- Science
- Published
- 2000-09-29
- Volume
- 289
- Issue
- 5488
- Pages
- 2354-2356
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2062306301
- Cited by
- 324
- References
- 16
- FWCI
- 5.29
- Type
- journal article
- Language
- en
- Open access
- closed
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