Bistable behaviour and medium-dependent post-translational regulation of the tryptophanase operon regulatory pathway in Echerichia coli.

ABSTRACT: The present work is aimed at studying the dynamic behaviour of the tryptopnanase (tna) operon, which encodes the proteins necessary to uptake and metabolise tryptophan to use it as a carbon source in the absence of glucose. To this end, we designed a micro-bioreactor capable of driving a bacterial culture to a stationary state. This allowed us to explore (at the single cell level) the tna operon steady-state dynamics under multiple culture conditions. Our experimental results suggest that the tna operon is bistable for a specific range of environmental tryptophan and glucose concentrations, and evidence that both reagents play a role on the activation of the enzyme in charge of metabolising tryptophan: tryptophanase (TnaA). Based on our experimental data and the already known regulatory me

SUBMITTER: Orozco-Gomez DI 

PROVIDER: S-EPMC6443796 | biostudies-literature | 2019 Apr

REPOSITORIES: biostudies-literature