Drupal-Biblio17<style face="normal" font="default" size="100%">Two functions of the C-terminal domain of Escherichia coli Rob: mediating "sequestration-dispersal" as a novel off-on switch for regulating Rob's activity as a transcription activator and preventing degradation of Rob by Lon protease.</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Inducible protein degradation in Bacillus subtilis using heterologous peptide tags and adaptor proteins to target substrates to the protease ClpXP.</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Characterization of TetD as a transcriptional activator of a subset of genes of the Escherichia coli SoxS/MarA/Rob regulon.</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Genetic evidence for pre-recruitment as the mechanism of transcription activation by SoxS of Escherichia coli: the dominance of DNA binding mutations of SoxS.</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Proteolytic degradation of Escherichia coli transcription activators SoxS and MarA as the mechanism for reversing the induction of the superoxide (SoxRS) and multiple antibiotic resistance (Mar) regulons.</style>Drupal-Biblio17<style face="normal" font="default" size="100%">A comprehensive alanine scanning mutagenesis of the Escherichia coli transcriptional activator SoxS: identifying amino acids important for DNA binding and transcription activation.</style>Drupal-Biblio17<style face="normal" font="default" size="100%">Evidence for "pre-recruitment" as a new mechanism of transcription activation in Escherichia coli: the large excess of SoxS binding sites per cell relative to the number of SoxS molecules per cell.</style>