期刊
SCIENCE
卷 289, 期 5488, 页码 2354-2356出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.289.5488.2354
关键词
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资金
- NIAID NIH HHS [AI-16892] Funding Source: Medline
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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