Residual guanosine 3‘,5‘-bispyrophosphate synthetic activity of relA null mutants can be eliminated by spoT null mutations.
Open Access
- 1 March 1991
- journal article
- abstracts
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 266 (9) , 5980-5990
- https://doi.org/10.1016/s0021-9258(19)67694-5
Abstract
No abstract availableKeywords
This publication has 54 references indexed in Scilit:
- The physiology of stringent factor (ATP: GTP 3′-diphosphotransferase) in Escherichia coliBiochimie, 1986
- Improved M13 phage cloning vectors and host strains: nucleotide sequences of the M13mpl8 and pUC19 vectorsGene, 1985
- Degradation of Guanosine 3'-diphosphate 5'-diphosphate in vitro by the spoT Gene Product of Escherichia coliEuropean Journal of Biochemistry, 1978
- In vitro degradation of guanosine tetraphosphate (ppGpp) by an enzyme associated with the ribosomal fraction from Escherichia coliFEBS Letters, 1977
- Cyclic AMP can replace the relA-dependent requirement for derepression of acetohydroxy acid synthase in E. coli K-12Cell, 1977
- Analysis of the relA Gene Product of Escherichia coliEuropean Journal of Biochemistry, 1977
- A rapid test for the rel a mutation in E. coliBiochemical and Biophysical Research Communications, 1976
- A ribosome-independent, soluble stringent factor-like enzyme isolated from a Bacillus brevisBiochemistry, 1976
- Altered metabolism of the guanosine tetraphosphate, ppGpp, in mutants of E. coliCell, 1974
- MSI and MSII made on Ribosome in Idling Step of Protein SynthesisNature, 1972