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Science 27 July 2001: Vol. 293. no. 5530, pp. 705 - 708 DOI: 10.1126/science.1061315
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Reports
Role of Inorganic Polyphosphate in Promoting Ribosomal Protein Degradation by the Lon Protease in E. coli
Akio Kuroda,1*
Kazutaka Nomura,1
Ryo Ohtomo,2
Junichi Kato,1
Tsukasa Ikeda,1
Noboru Takiguchi,1
Hisao Ohtake,1
Arthur Kornberg2
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.
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.
*
To whom correspondence should be addressed. E-mail:
akuroda{at}hiroshima-u.ac.jp
Read the Full Text
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