Disease relevance of ECs1148

• An unsuspected autoregulatory pathway involving apocytochrome TorC and sensor TorS in Escherichia coli [1].

High impact information on ECs1148

• This operon is positively regulated, in the presence of trimethylamine N-oxide, by a four-step phosphorelay involving the TorS sensor and the TorR response regulator [2].
• As regulation of these genes by the TorS/TorR system does not depend on pH modification but rather on the presence of TMAO, we propose that E. coli anticipates alkalinization of the medium due to TMA production by base-resistance gene activation and acid-resistance gene repression [3].
• An unorthodox sensor protein (TorS) mediates the induction of the tor structural genes in response to trimethylamine N-oxide in Escherichia coli [4].
• The TorS histidine kinase is an unorthodox sensor that contains a receiver and a C-terminal alternative transmitter domain in addition to the domains found in most sensors [4].
• Transphosphorylation of the TorR response regulator requires the three phosphorylation sites of the TorS unorthodox sensor in Escherichia coli [5].

Biological context of ECs1148

• Moreover, the N-terminal half of apoTorC played no role in this control but the immature C-terminal domain of TorC strongly down-regulated the tor operon and interacted with the TorS detector region [1].
• This strongly suggests that TorS is a multimer in which intermolecular phosphorylation occurs [5].

Associations of ECs1148 with chemical compounds

• Expression of the tor operon is positively controlled by the TorS/TorR phosphorelay system in response to TMAO availability and negatively regulated by apocytochrome TorC [1].

Analytical, diagnostic and therapeutic context of ECs1148

• The histidine phosphorylation sites of each TorS transmitter domain and the aspartate phosphorylation site of the TorS receiver were individually changed by site-directed mutagenesis [5].

References