The RF1 antibody targets Ribosome Release Factor 1 (RF1), a protein critical for terminating protein synthesis in prokaryotes. RF1 recognizes stop codons UAA and UAG during translation, facilitating the release of nascent polypeptide chains from ribosomes by hydrolyzing the ester bond linking the completed protein to tRNA. Discovered in the 1960s-70s, RF1 works alongside RF2 (which recognizes UAA/UGA) and is structurally distinct from eukaryotic release factors, making it a potential target for antibacterial therapies.
Research on RF1 has advanced understanding of translation termination mechanisms. Structural studies using X-ray crystallography and cryo-EM revealed that RF1 adopts a conserved conformation when bound to ribosomes, employing specific domains to decode stop signals and catalyze peptide release. Its GTPase activity, though less understood, appears to coordinate with ribosomal subunits during termination.
RF1 antibodies are primarily used as research tools to investigate bacterial translation processes, antibiotic resistance mechanisms, and microbial physiology. Recent studies explore RF1 inhibition as an antimicrobial strategy, particularly against multidrug-resistant pathogens. Additionally, these antibodies aid in structural biology studies mapping ribosomal interactions and evolutionary analyses comparing termination factors across species. While primarily confined to basic research, RF1 antibodies hold translational potential for developing novel antibiotics targeting protein synthesis in pathogenic bacteria.