Inhibitors | Comment | Organism | Structure |
---|---|---|---|
RecA | stimulates self-cleavage of a scissile peptide bond between Ala84 and Gly85, thereby de-activating LexA. Data indicate that the RecA filament predominately induces self-cleavage in one monomer of the LexA dimer and that the resulting LexALexA/CTD heterodimer is an inactive intermediate, exhibiting weaker DNA binding. RecA cannot induce self-cleavage in LexA that is bound to target DNA operator sites. In unbound LexA, the DNA-binding domains sample different conformations. One of these conformations is captured when LexA is bound to operator targets and this precludes interaction by RecA | Escherichia coli |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Escherichia coli | - |
- |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | RecA stimulates self-cleavage of a scissile peptide bond between Ala84 and Gly85, thereby de-activating LexA. RecA cannot induce self-cleavage in LexA that is bound to target DNA operator sites. In unbound LexA, the DNA-binding domains sample different conformations. One of these conformations is captured when LexA is bound to operator targets and this precludes interaction by RecA. Hence, the conformational flexibility of unbound LexA is the key element in establishing a co-ordinated SOS response. While LexA exhibits diverse dissociation rates from operators, it interacts extremely rapidly with DNA target sites. Modulation of LexA activity changes the occurrence of persister cells in bacterial populations | Escherichia coli | ? | - |
? |