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Inorganic polyphosphate and the induction of rpoS expression.

Inorganic polyphosphate [poly(P)] levels in Escherichia coli were reduced to barely detectable concentrations by expression of the plasmid-borne gene for a potent yeast exopolyphosphatase [poly(P)ase]. As a consequence, resistance to H2O2 was greatly diminished, particularly in katG (catalase HPI) mutants, implying a major role for the other catalase, the stationary-phase KatE (HPII), which is rpoS dependent. Resistance was restored to wild-type levels by complementation with plasmids expressing ppk, the gene for PPK [the polyphosphate kinase that generates poly(P)]. Induction of expression of both katE and rpoS (the stationary-phase sigma factor) was prevented in cells in which the poly(P)ase was overproduced. Inasmuch as this inhibition by poly(P)ase did not affect the levels of the stringent-response guanosine nucleotides (pppGpp and ppGpp) and in view of the capacity of additional rpoS expression to suppress the poly(P)ase inhibition of katE expression, a role is proposed for poly(P) in inducing the expression of rpoS.[1]

References

  1. Inorganic polyphosphate and the induction of rpoS expression. Shiba, T., Tsutsumi, K., Yano, H., Ihara, Y., Kameda, A., Tanaka, K., Takahashi, H., Munekata, M., Rao, N.N., Kornberg, A. Proc. Natl. Acad. Sci. U.S.A. (1997) [Pubmed]
 
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