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J. Biol. Chem., Vol. 263, Issue 30, 15699-15704, 10, 1988
S Metzger, IB Dror, E Aizenman, G Schreiber, M Toone, JD Friesen, M Cashel and G Glaser
The relA gene product of Escherichia coli is known to be responsible for
the synthesis of guanosine 3',5'-bispyrophosphate (ppGpp) during the
stringent response to amino acid starvation. This report presents the
sequence of the relA gene region and assignment of its 743-codon open
reading frame by the following criteria: 1) genetic complementation of
ppGpp synthesis in a relaxed (relA1) mutant during the stringent response;
2) changes in 3-aminotriazole resistance during growth to mimic a relA+
phenotype; 3) verification of the presence of an amber codon at the normal
carboxyl terminus of the relA gene; and 4) immunological assays of
expression of the RelA protein. The apparent molecular mass of the cloned
relA gene product is calculated to be 83,856 daltons and as visualized by
immunoblotting is identical to that of the previously characterized
protein. A promoter has been identified that directs relA gene
transcription towards the pyrG gene, in a counterclockwise direction on the
E. coli chromosome. Genomic Southern blot analyses verify that the relA
regions cloned and subjected to nucleotide sequence analysis correspond to
homologous regions on the E. coli chromosome.
The nucleotide sequence and characterization of the relA gene of Escherichia coli
Department of Cellular Biochemistry, Hadassah Medical School, Hebrew University, Jerusalem, Israel.
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