EC Number   |
Activating Compound |
Reference |
|---|
   3.4.21.88 | GIL01 phage gp7 protein |
LexA is unable to efficiently repress GIL01 transcription unless the small phage-encoded protein gp7 is also present. Phage protein gp7 forms a stable complex with LexA that enhances LexA binding to phage and cellular SOS sites and interferes with RecA-mediated auto-cleavage of LexA, the key step in the initiation of the SOS response. Gp7 does not bind DNA, alone or when complexed with LexA. Gp7 interacts with LexA at dinBox1 and dinBox1b and Gp7 induces a LexA conformation that favors DNA binding but disfavors LexA auto-cleavage, thereby altering the dynamics of the cellular SOS response. Gp7 increases the apparent binding capacity of LexA for din-Box1 and dinBox1b. Gp7 represses promoter P1 and prevents its SOS induction in vivo. gp7 repression of P1 is LexA-dependent |
754924 |
| 3.4.21.88 | more |
LexA activation by activated RecA-dependent proteolytic self-cleavage |
754924 |
| 3.4.21.88 | more |
overexpression of the SOS-inducible tisAB gene leads to higher levels of LexA repressor both in unirradiated strain AB1157 and throughout the induction period causing a delay in recA mRNA induction |
700498 |
| 3.4.21.88 | more |
serine-119 of repressor LexA activates |
29802 |
| 3.4.21.88 | more |
the ssDNA-RecA filament interacts with LexA and activates a self-cleaving activity in LexA |
696422 |
| 3.4.21.88 | RecA |
RecA binds to and polymerizes on single-stranded DNA, which is a product of DNA damage. As a complex, it activates the autocleavage of LexA thereby lifting repression of SOS genes under DNA-damage conditions |
755567 |
| 3.4.21.88 | RecA protein |
RecA protein and single-stranded DNA are required for activity being attributed to a Ser/Lys dyad. The LexA protein represses the SOS regulon, which regulates the genes involved in DNA repair. In the presence of single-stranded DNA, the RecA protein interacts with repressor LexA, causing it to undergo an autocatalytic cleavage which disrupts the DNA-binding part of the repressor, and inactivates it. The consequent derepression of the SOS regulon leads to DNA repair |
29801, 29803 |
| 3.4.21.88 | single-stranded DNA |
RecA protein and single-stranded DNA are required for activity being attributed to a Ser/Lys dyad. The LexA protein represses the SOS regulon, which regulates the genes involved in DNA repair. In the presence of single-stranded DNA, the RecA interacts with repressor LexA, causing it to undergo an autocatalytic cleavage which disrupts the DNA-binding part of the repressor, and inactivates it. The consequent derepression of the SOS regulon leads to DNA repair |
29801 |
