In vitro synthesis of the first dipeptide of the beta subunit of Escherichia coli RNA polymerase.
- 1 August 1982
- journal article
- research article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 79 (15) , 4609-4612
- https://doi.org/10.1073/pnas.79.15.4609
Abstract
Plasmids pNF1337 and pNF1341, which contain part of the L10 operon including the RNA polymerase .beta.-subunit gene, were used as templates in vitro to investigate expression of the .beta.-subunit gene. For these studies, the synthesis of the 1st dipeptide of the .beta.-subunit, fMet-Val, was measured instead of that of the entire protein. By using this dipeptide system, the effects of RNA polymerase holoenzyme and L factor (nusA gene product) on fMet-Val synthesis was studied and the relative effects of the primary and secondary promoters in the L10 operon on expression of the .beta.-subunit gene were compared. The inhibitory effect of RNA polymerase on .beta.-subunit synthesis and the stimulatory effect of L factor occur before formation of the 1st dipeptide bond. In this in vitro system, the secondary promoters account for about 50% of the total fMet-Val synthesized. Although the primary promoter is sensitive to guanosine 5''-diphosphate 3''-diphosphate in vitro, the secondary promoters are not affected by this nucleotide.This publication has 29 references indexed in Scilit:
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