Recombination protein A (RecA) (RecA)

Recombination protein A (RecA) is a highly conserved bacterial enzyme that plays a central role in DNA repair and homologous recombination [1, 5]. It functions by forming a helical nucleoprotein filament on single-stranded DNA, which then searches for and invades homologous double-stranded DNA to facilitate strand exchange and repair [8, 9]. In addition to its recombinase activity, RecA acts as a co-protease that triggers the bacterial SOS response by stimulating the self-cleavage of the LexA repressor [11, 12]. This induction leads to the expression of over 40 genes involved in DNA repair, survival, and stress-induced mutagenesis, which often contributes to the development of antibiotic resistance [13, 17]. Consequently, RecA is an attractive therapeutic target for the development of antibiotic adjuvants designed to sensitize pathogens to existing drugs and prevent the emergence of multi-drug resistance [2, 10]. Small molecule inhibitors and peptides targeting RecA's ATPase activity or filament formation are currently being explored to attenuate the SOS response and enhance the efficacy of DNA-damaging antibiotics like fluoroquinolones [3, 18].

Other names

RecA protein [1, 8]Bacterial recombinase A [7, 10]DNA strand exchange protein [5, 9]Recombinase A [7, 10]

Inhibition of RecA ATPase activity, inhibition of RecA-ssDNA nucleoprotein filament formation, and blocking of the SOS response by preventing LexA cleavage [2, 3, 10, 13].