Key result
Charge-flip variant release factor proteins altered at conserved Glu residues trigger polypeptide release at noncognate stop and sense codons, mediating accurate docking in the ribosome.
Electrostatic interactions involving negative charges in domain C of bacterial release factors mediate accurate docking in the ribosome and stop codon recognition.
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No clinical implications yet; extends models of ribosomal release factor specificity.
Uno et al. (2002) studied this question. Charge-flip variant release factor (RF) proteins was evaluated on Polypeptide release at noncognate stop codons and sense codons. Charge-flip variant release factor proteins altered at conserved Glu residues trigger polypeptide release at noncognate stop and sense codons, mediating accurate docking in the ribosome.
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