Journal
SCIENCE
Volume 293, Issue 5530, Pages 705-708Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1061315
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Inorganic polyphosphate (polyp), a polymer of hundreds of phosphate (P-i) residues, accumulates in Escherichia coli in response to stresses, including amino acid starvation. Here we show that the adenosine 5'-triphosphate-dependent protease Lon formed a complex with polyp and degraded most of the ribosomal proteins, including S2, L9, and L13. Purified S2 also bound to polyp and formed a complex with Lon in the presence of polyP. Thus, polyP may promote ribosomal. protein degradation by the Lon protease, thereby supplying the amino acids needed to respond to starvation.
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