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Inorganic polyphosphate (polyP), a polymer of
hundreds of phosphate (Pi) residues, accumulates in
Escherichia coli in responseto stresses, including amino
acid starvation. Here we show thatthe adenosine
5'-triphosphate-dependent protease Lon formed acomplex with polyP and
degraded most of the ribosomal proteins,including S2, L9, and L13.
Purified S2 also bound to polyP andformed a complex with Lon in the
presence of polyP. Thus, polyPmay 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
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