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Originally published In Press as doi:10.1074/jbc.M209881200 on November 5, 2002

J. Biol. Chem., Vol. 278, Issue 2, 968-973, January 10, 2003
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Underproduction of sigma 70 Mimics a Stringent Response
A PROTEOME APPROACH*

Lisa U. Magnusson, Thomas Nyström, and Anne FarewellDagger

From the Department of Cell and Molecular Biology-Microbiology, Göteborg University, Box 462, 405 30 Göteborg, Sweden

When Escherichia coli cells enter stationary phase due to carbon starvation the synthesis of ribosomal proteins is rapidly repressed. In a Delta relA Delta spoT mutant, defective in the production of the alarmone guanosine tetraphosphate (ppGpp), this regulation of the levels of the protein synthesizing system is abolished. Using a proteomic approach we demonstrate that the production of the vast majority of detected E. coli proteins are decontrolled during carbon starvation in the Delta relA Delta spoT strain and that the starved cells behave as if they were growing exponentially. In addition we show that the inhibition of ribosome synthesis by the stringent response can be qualitatively mimicked by artificially lowering the levels of the housekeeping sigma  factor, sigma 70. In other words, genes encoding the protein-synthesizing system are especially sensitive to reduced availability of sigma 70 programmed RNA polymerase. This effect is not dependent on ppGpp since lowering the levels of sigma 70 gives a similar but less pronounced effect in a ppGpp0 strain. The data is discussed in view of the models advocating for a passive control of gene expression during stringency based on alterations in RNA polymerase availability.


* The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed. Tel.: 46-0-31-7732567; Fax: 46-0-31-7732599; E-mail: anne.farewell@gmm.gu.se.


Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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