Single-stranded DNA-binding protein A (SsbA) (SaSsbA)

Single-stranded DNA-binding protein A (SsbA) from Staphylococcus aureus is an essential protein involved in maintaining genome integrity and facilitating DNA metabolism [1.3.1, 1.3.5]. It functions as a stable homotetramer that binds with high affinity and little sequence specificity to single-stranded DNA (ssDNA) intermediates generated during replication, repair, and recombination [1.3.1, 1.5.1]. By coating these ssDNA regions, SaSsbA protects them from nucleolytic degradation and prevents the formation of inhibitory secondary structures, thereby ensuring the smooth progression of DNA polymerase and other replication machinery [1.3.1, 1.3.5]. In S. aureus, SsbA is the primary SSB and is critical for the survival of the pathogen, making it a significant target for the development of novel antibacterial agents [1.3.1, 1.4.1]. Research has identified several small molecules, such as the flavonoid myricetin and the compound NSC5426 (9-methyl-2,3,7-trihydroxy-6-fluorone), that can potently inhibit its DNA-binding activity [1.3.5]. These inhibitors disrupt essential cellular processes, leading to bacterial cell death, and offer a potential strategy for treating multi-drug resistant infections like MRSA [1.3.5, 1.4.2].

Other names

SSBSsbASingle-strand DNA-binding proteinSAAV_0334Staphylococcus aureus SSB

Inhibition of single-stranded DNA binding