Characterization of the relA1 mutation and a comparison of relA1 with new relA null alleles in Escherichia coli.

@article{Metzger1989CharacterizationOT,
  title={Characterization of the relA1 mutation and a comparison of relA1 with new relA null alleles in Escherichia coli.},
  author={Shulamit Metzger and Gerhard Schreiber and Einat Aizenman and Michael Cashel and G. Glaser},
  journal={The Journal of biological chemistry},
  year={1989},
  volume={264 35},
  pages={21146-52}
}
The most widely studied "relaxed" mutant of the relA locus, the relA1 allele, is shown here to consist of an IS2 insertion between the 85th and 86th codons of the otherwise wild-type relA structural gene, which normally encodes a 743-amino acid (84 kDa) protein. The RelA protein is a ribosome-dependent ATP:GTP (GDP) pyrophosphoryltransferase that is activated during the stringent response to amino acid starvation and thereby occasions the accumulation of guanosine 3',5'-bispyrophosphate (ppGpp… CONTINUE READING
43 Citations
0 References
Similar Papers

Citations

Publications citing this paper.
Showing 1-10 of 43 extracted citations

Similar Papers

Loading similar papers…