Summary:
HicB acts as the antitoxin of the HicA-HicB toxin-antitoxin system, and it also regulates the transcription of the operon that encodes the toxin-antitoxin system. HicB recognizes and binds an inverted repeat DNA sequence to regulate transcription, suggesting that HicB binds to DNA as a dimer [1]. An HTH motif has been identified in the C terminus of HicB [1].
Overexpression of HicA induces mRNA cleavage and growth inhibition, but not cell death. Expression of HicB neutralizes the effect of HicA [2].
The loss of HicB downregulates the extracytoplasmic stress response mediated by σE and the production of outer membrane vesicles. It reduces the cellular levels of DegP and Spy and downregulates the Cpx response independently of CpxR [3].
hicB insertion mutants suppress the essential nature of |FRAME: RPOE-MONOMER σE| [3].
The mRNA interferase activity of the cognate toxin HicA appears to be responsible for this effect; overexpression of any one of three RNA interferase toxins, HicA, HigB or YafQ, suppresses the essentiality of σ
E [4].
hicB mutants have no detectable growth defect, but are more sensitive to envelope stress
[3].
hicAB expression is induced by nutrient starvation
[2].
The crystal structures of the isolated HicB antitoxin and full-length HicAB complex were determined
[5] HicAB and HicB interact differently with the promoter regions
[5] Toxin-antitoxin interactions are conserved among HicAB orthologs
[5] HicB forms a stable DNA-binding module and interacts in a canonical way with a conserved histidine residue in HicA, despite the presence of an HTH-type DNA-binding domain
[5] It is probable that activation of the HicAB TA complex is required for the degradation of the HicB antitoxin by the stress-induced protease Lon, which releases the toxin
[2]
Review:
[6]
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