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Streptomyces nucleotide 3'-pyrophosphokinase are insensitive to stringent control
1Graduate School of Genetic Resources Technology, Kyushu University, Fukuoka, Japan.
Journal of Basic Microbiology
|January 1, 1989
Summary
Streptomyces morookaensis nucleotide 3'-pyrophosphokinase synthesized GTP- and ATP-3'-pyrophosphate. This enzyme activity was unaffected by a tRNA-poly A, G, U mixture, suggesting it does not play a role in stringent control.
Area of Science:
- Microbiology
- Molecular Biology
- Biochemistry
Background:
- Bacterial stringent control is a crucial cellular response to stress, mediated by stringent factors.
- Nucleotide 3 -pyrophosphokinases are enzymes involved in nucleotide metabolism.
Purpose of the Study:
- To investigate the role of Streptomyces morookaensis nucleotide 3 -pyrophosphokinase in cellular stringent control.
- To determine if this enzyme functions similarly to bacterial stringent factors.
Main Methods:
- In vitro synthesis of GTP- and ATP-3 -pyrophosphate by purified Streptomyces morookaensis nucleotide 3 -pyrophosphokinase.
- Assessing the effect of a ribosome-deacylated tRNA-poly A, G, U mixture on enzyme activity.
Main Results:
- The synthesis of GTP- and ATP-3 -pyrophosphate by Streptomyces morookaensis nucleotide 3 -pyrophosphokinase was minimally impacted by the presence of the tRNA-poly A, G, U mixture.
- This indicates a lack of significant interaction with components typically involved in stringent control.
Conclusions:
- Streptomyces morookaensis nucleotide 3 -pyrophosphokinases do not appear to be involved in cellular stringent control.
- Unlike bacterial stringent factors, these enzymes likely have a different physiological role in Streptomyces.