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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
Underproduction of 70 Mimics a Stringent
Response
A PROTEOME APPROACH*
Lisa U.
Magnusson,
Thomas
Nyström, and
Anne
Farewell
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 relA
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 relA 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 factor, 70. In other
words, genes encoding the protein-synthesizing system are especially
sensitive to reduced availability of 70 programmed RNA
polymerase. This effect is not dependent on ppGpp since lowering the
levels of 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.
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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Copyright © 2003 by the American Society for Biochemistry and Molecular Biology.
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