Escherichia coli Leucine-Responsive Regulatory Protein Bridges DNA <i>In Vivo</i> and Tunably Dissociates in the Presence of Exogenous Leucine.

ABSTRACT: Feast-famine response proteins are a widely conserved class of global regulators in prokaryotes, the most highly studied of which is the Escherichia coli leucine-responsive regulatory protein (Lrp). Lrp senses the environmental nutrition status and subsequently regulates up to one-third of the genes in E. coli, either directly or indirectly. Lrp exists predominantly as octamers and hexadecamers (16mers), where leucine is believed to shift the equilibrium toward the octameric state. In this study, we analyzed the effects of three oligomerization state mutants of Lrp in terms of their ability to bind to DNA and regulate gene expression in response to exogenous leucine. We find that oligomerization beyond dimers is required for Lrp's regulatory activity and that, contrary to previous speculat

SUBMITTER: Ziegler CA 

PROVIDER: S-EPMC10127797 | biostudies-literature | 2023 Apr

REPOSITORIES: biostudies-literature