Abstract
DNA replication is an essential process. Although the fundamental strategies to duplicate chromosomes are similar in all free-living organisms, the enzymes of the three domains of life that perform similar functions in DNA replication differ in amino acid sequence and their three-dimensional structures. Moreover, the respective proteins generally utilize different enzymatic mechanisms. Hence, the replication proteins that are highly conserved among bacterial species are attractive targets to develop novel antibiotics as the compounds are unlikely to demonstrate off-target effects. For those proteins that differ among bacteria, compounds that are species-specific may be found. Escherichia coli has been developed as a model system to study DNA replication, serving as a benchmark for comparison. This review summarizes the functions of individual E. coli proteins, and the compounds that inhibit them.
Highlights
Penicillin is produced by a specific species of mold named Penicillium chrysogenum and is believed to provide a growth advantage to the organism when competing in nature with bacteria for nutrients
In the decades of research that have passed since, we know that the process in all domains of life is enzymatically mediated by macromolecular machines that act dynamically with the DNA as it is being copied
Because the individual proteins of bacteria of these nanomachines are substantially different from their eukaryotic counterparts, novel compounds that inhibit bacterial DNA replication are unlikely to affect DNA replication in eukaryotic cells, avoiding the problem of toxicity in humans [289]
Summary
Some smaller-cap companies have made efforts into the newest generation of antibiotics. DnaA, DnaC, and the δ and δ’ subunits of DNA polymerase III contain distinguishing amino acid motifs of the AAA+ family of ATPases The functions of these E. coli proteins in DNA replication and compounds that inhibit individual proteins, including inhibitors of DNA polymerases of. Small aromatic compounds named CFAM, BCBP, BOTP, and MPTA have been identified that interfere with bacterial growth by inhibiting the interaction of SSB with Exonuclease I, RecQ and PriA DNA helicase [27,28].
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