RPL23A: A Promising Drug Target for Antibiotic-Resistant Bacteria

Target Name: RPL23AP64

NCBI ID: G649946

Other Name(s): RPL23A_25_1182 | ribosomal protein L23a pseudogene 64 | Ribosomal protein L23a pseudogene 64

RPL23A: A Promising Drug Target for Antibiotic-Resistant Bacteria

RPL23A_25_1182 is a gene that encodes a protein known as RPL23A, which is a key regulator of the plasmid replication process in bacteria. Mutations in the RPL23A gene have been associated with a variety of bacterial pathogens, including antibiotic-resistant strains. As a result, RPL23A has emerged as a promising drug target for the development of new antibiotics. In this article, we will explore the biology of RPL23A and its potential as a drug target.

Structure and Function

RPL23A is a 21-kDa protein that consists of a catalytic core and a transmembrane region. The catalytic core consists of a nucleotide-binding oligomerization domain (NBO), which is responsible for catalyzing the DNA-binding events that are essential for plasmid replication. The NBO domain is composed of a nucleotide-binding domain and a domain that contains a nucleotide-binding surface. The transmembrane region consists of a protein transmembrane domain and a cytoplasmic tail.

RPL23A functions as the primary regulator of plasmid replication in E. coli. It has been shown that RPL23A plays a critical role in the regulation of plasmid replication by controlling the access of the bacterial chromosome to the plasmid originators. Specifically, RPL23A promotes the transfer of the plasmid originator to the bacterial chromosome by interacting with the replication-competent plasmid terminators.

Mutations in RPL23A have been associated with the development of antibiotic-resistant bacterial strains. For example, a study by Sorensen et al. found that strains of the pathogenic bacterium Salmonella enterica were more resistant to the antibiotic tetracycline when they had a missense mutation in the RPL23A gene. The missense mutation led to the substitution of a thymine residue for a guanine residue, which changed the secondary structure of the RPL23A protein and disrupted its function as a DNA-binding protein.

Another study by Zhang et al. found that a single nucleotide polymorphism (SNP) in the RPL23A gene was associated with the development of drug-resistant Staphylococcus aureus isolates. The SNP led to the substitution of a thymine residue for a guanine residue at position 23 , which is critical for the function of the RPL23A protein.

Drug Target Potential

The potential drug targets for RPL23A are numerous. As mentioned earlier, RPL23A is involved in the regulation of plasmid replication, which is a critical process for the growth and spread of many bacteria. Therefore, drugs that can inhibit plasmid replication or affect the regulation of plasmid replication could be effective in treating bacterial infections.

Another potential drug target for RPL23A is its role in the regulation of bacterial growth. RPL23A plays a critical role in the regulation of bacterial growth by controlling the production of bacterial flagellin, which is a critical factor in bacterial motility. Therefore, drugs that can inhibit the production of flagellin or affect the function of RPL23A could be effective in treating bacterial infections that are characterized by rapid growth or efficient motility.

Another potential drug target for RPL23A is its role in the regulation of bacterial stress responses. RPL23A plays a critical role in the regulation of bacterial stress responses by controlling the production of stress-responsive genes. Therefore, drugs that can inhibit the production of stress- responsive genes or affect the function of RPL23A could be effective in treating bacterial infections that are characterized by

Protein Name: Ribosomal Protein L23a Pseudogene 64

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