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

Author:

Kuroda Akio1,Nomura Kazutaka1,Ohtomo Ryo2,Kato Junichi1,Ikeda Tsukasa1,Takiguchi Noboru1,Ohtake Hisao1,Kornberg Arthur2

Affiliation:

1. Department of Molecular Biotechnology, Graduate School of Advanced Sciences of Matter, Hiroshima University, 1-4-1 Kagamiyama, Hiroshima 739-8527, Japan.

2. Department of Biochemistry, Stanford University, Stanford, CA 94305–5307, USA.

Abstract

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.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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