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Role of Inorganic Polyphosphate in Promoting Ribosomal Protein Degradation by the Lon Protease in E. coli

Science  27 Jul 2001:
Vol. 293, Issue 5530, pp. 705-708
DOI: 10.1126/science.1061315

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Abstract

Inorganic polyphosphate (polyP), a polymer of hundreds of phosphate (Pi) residues, accumulates inEscherichia 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.

  • * To whom correspondence should be addressed. E-mail: akuroda{at}hiroshima-u.ac.jp

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