A Specificity-Enhancing Factor for the ClpXP Degradation Machine

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-depe...

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Veröffentlicht in:Science (American Association for the Advancement of Science) 2000-09, Vol.289 (5488), p.2354-2356
Hauptverfasser: Levchenko, Igor, Seidel, Meredith, Sauer, Robert T., Baker, Tania A.
Format: Artikel
Sprache:eng
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Zusammenfassung: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.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.289.5488.2354