Role of inorganic polyphosphate in promoting ribosomal protein degradation by the Lon protease in E. coli.

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.

• Authors: A Kuroda, K Nomura, R Ohtomo, J Kato, T Ikeda, N Takiguchi, H Ohtake, A Kornberg
• Journal: Science (New York, N.Y.) (Science) Vol. 293 Issue 5530 Pg. 705-8 (Jul 27 2001) ISSN: 0036-8075 [Print] United States
• PMID: 11474114 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, P.H.S.)

Chemical References

• Amino Acids
• Bacterial Proteins
• Escherichia coli Proteins
• Heat-Shock Proteins
• Polyphosphates
• Ribosomal Proteins
• ribosomal protein L9
• ribosomal protein S2
• Adenosine Triphosphate
• Phosphotransferases (Phosphate Group Acceptor)
• polyphosphate kinase
• ATP-Dependent Proteases
• Serine Endopeptidases
• Lon protein, E coli
• Protease La
• Endopeptidase Clp
• Adenosine Triphosphatases

Topics

• ATP-Dependent Proteases
• Adaptation, Physiological
• Adenosine Triphosphatases (genetics, metabolism)
• Adenosine Triphosphate (metabolism)
• Amino Acid Sequence
• Amino Acids (metabolism)
• Bacterial Proteins (chemistry, metabolism)
• Endopeptidase Clp
• Escherichia coli (genetics, metabolism)
• Escherichia coli Proteins
• Heat-Shock Proteins (genetics, metabolism)
• Molecular Sequence Data
• Mutation
• Phosphotransferases (Phosphate Group Acceptor) (genetics, metabolism)
• Polyphosphates (metabolism)
• Protease La
• Ribosomal Proteins (chemistry, metabolism)
• Ribosomes (metabolism)
• Serine Endopeptidases (genetics, metabolism)