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

• Published in: Science (American Association for the Advancement of Science) 2001-07, Vol.293 (5530), p.705-708
• Main Authors: Kuroda, Akio, Nomura, Kazutaka, Ohtomo, Ryo, Kato, Junichi, Ikeda, Tsukasa, Takiguchi, Noboru, Ohtake, Hisao, Kornberg, Arthur
• Format: Article
• Language: English
• Subjects: Adaptation, Physiological; Adenosine Triphosphatases - genetics; Adenosine Triphosphatases - metabolism; Adenosine Triphosphate - metabolism; Amino Acid Sequence; Amino acids; Amino Acids - metabolism; ATP-Dependent Proteases; Bacteria; Bacterial Proteins - chemistry; Bacterial Proteins - metabolism; Bacteriology; Biological and medical sciences; Cytology; DNA; Endopeptidase Clp; Enzymes; Escherichia coli; Escherichia coli - genetics; Escherichia coli - metabolism; Escherichia coli Proteins; Fundamental and applied biological sciences. Psychology; Growth, nutrition, cell differenciation; Heat-Shock Proteins - genetics; Heat-Shock Proteins - metabolism; Individualized Instruction; Lon protein; Microbiology; Molecular Biology; Molecular Sequence Data; Mutation; Phosphates; Phosphorus; Phosphotransferases (Phosphate Group Acceptor) - genetics; Phosphotransferases (Phosphate Group Acceptor) - metabolism; Polymers; polyphosphate; Polyphosphates; Polyphosphates - metabolism; Protease La; Proteins; Ribosomal proteins; Ribosomal Proteins - chemistry; Ribosomal Proteins - metabolism; Ribosomes; Ribosomes - metabolism; RNA; Serine Endopeptidases - genetics; Serine Endopeptidases - metabolism; Starvation; Yeasts
• ISSN: 0036-8075; 1095-9203
• DOI: 10.1126/science.1061315

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.