| Literature DB >> 11009422 |
I Levchenko1, M Seidel, R T Sauer, T A Baker.
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.Mesh:
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Year: 2000 PMID: 11009422 DOI: 10.1126/science.289.5488.2354
Source DB: PubMed Journal: Science ISSN: 0036-8075 Impact factor: 47.728