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J. Biol. Chem., Vol. 266, Issue 6, 3760-3767, 02, 1991
G Schreiber, S Metzger, E Aizenman, S Roza, M Cashel and G Glaser
Intracellular levels of guanosine 3',5'-bispyrophosphate (ppGpp) governed
by the relA gene are normally regulated by aminoacyl-tRNA availability for
protein synthesis. An experimental system is described in which cellular
levels of ppGpp are controlled instead by induction of plasmid pKK223-3
derivatives with the relA structural gene, or portions thereof, under
control of the Ptac promoter. In amino acid- rich media,
isopropyl-1-thio-beta-D-galactopyranoside induction of transcription of the
wild type relA gene in pSM10 yields about a 100- fold overexpression of a
metabolically stable, full length (743 amino acid) RelA protein to levels
approximating the number of cellular ribosomes. This overexpression is
accompanied by a roughly parallel and relC-dependent elevation of ppGpp
levels. Induction of a relA gene deletion mutant in pSM11 containing 455
amino-terminal amino acids results in much lower levels of expression of a
metabolically unstable 55-kDa protein and elevated ppGpp levels that are
almost equivalent to induced pSM10 and are relC-independent. Induction of a
larger deletion in pSM12 containing 331 amino-terminal amino acids does not
provoke ppGpp accumulation. We are able to elicit high levels of ppGpp
without changing nutritional abundance and without massive overexpression
of the RelA protein by inducing the metabolically unstable, truncated RelA
protein. We find the effects of elevated ppGpp levels to include a slowing
of growth, an inhibition of stable RNA accumulation, an inhibition of
cellular rrn P1 promoter activities as measured by primer extension, and
changes in the pattern of gene expression viewed by two- dimensional
electrophoresis of cellular proteins.
Overexpression of the relA gene in Escherichia coli
Department of Cellular Biochemistry, Hadassah Medical School, Hebrew University, Jerusalem, Israel.
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