Role of inorganic polyphosphate in promoting ribosomal protein degradation by the Lon protease in E. coli |
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Authors: | Kuroda A Nomura K Ohtomo R Kato J Ikeda T Takiguchi N Ohtake H Kornberg A |
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Affiliation: | Department of Molecular Biotechnology, Graduate School of Advanced Sciences of Matter, Hiroshima University, 1-4-1 Kagamiyama, Hiroshima 739-8527, Japan. akuroda@hiroshima-u.ac.jp |
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Abstract: | Inorganic polyphosphate (polyP), a polymer of hundreds of phosphate (Pi) 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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