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The 30S subunit is the target of antibiotics such as tetracycline and gentamicin. [11] These antibiotics specifically target the prokaryotic ribosomes, hence their usefulness in treating bacterial infections in eukaryotes. Tetracycline interacts with H27 in the small subunit as well as binding to the A-site in the large subunit. [11]
The HTH motifs have mostly hydrophobic interactions with major grooves of the target DNA. [1] Binding of TetR to its target DNA sequence causes changes in both the DNA and TetR. [7] TetR causes widening of the major grooves as well as kinking of the DNA; one helix of the HTH motif of TetR adopts a 3 10 helical turn as the result of complex DNA ...
These viral DNA sequences enable the nuclease to target foreign (viral) rather than self (bacterial) DNA. [ 205 ] Although the function of CRISPR-Cas9 in nature is to protect bacteria, the DNA sequences in the CRISPR component of the system can be modified so that the Cas9 nuclease targets bacterial resistance genes or bacterial virulence genes ...
The following antibiotics bind to the 30S subunit of the ribosome: Aminoglycosides [17] Tetracyclines [17] The following antibiotics bind to the 50S ribosomal subunit: Chloramphenicol [17] Clindamycin [17] Linezolid [17] (an oxazolidinone) Macrolides [17] Telithromycin [17] Streptogramins [17] Retapamulin [18]
As human and bacteria both have ribosomes, streptomycin has significant side effects in humans. At low concentrations, however, streptomycin inhibits only bacterial growth. [18] Streptomycin is an antibiotic that inhibits both Gram-positive and Gram-negative bacteria, [19] and is therefore a useful broad-spectrum antibiotic.
Tetracycline antibiotics are protein synthesis inhibitors. [22] They inhibit the initiation of translation in variety of ways by binding to the 30S ribosomal subunit, which is made up of 16S rRNA and 21 proteins. They inhibit the binding of aminoacyl-tRNA to the mRNA translation complex.
Scientists say they have developed a new type of antibiotic to treat a bacteria that is resistant to most current antibiotics and kills a large percentage of people with an invasive infection.
A well-known member of this antibiotic class, chloramphenicol, acts by inhibiting peptide bond formation, with recent 3D-structural studies showing two different binding sites depending on the species of ribosome. Numerous mutations in domains of the 23S rRNA with Peptidyl transferase activity have resulted in antibiotic resistance.