A single mutation in 16S rRNA that affects mRNA binding and translation-termination.
A single base change in 16S rRNA (C726 to G) has previously been shown to have a dramatic effect on protein synthesis in E. coli (1). This paper more specifically details the effects of the mutation on mRNA binding and translation-termination. The in vitro technique of toeprinting (2) was used to demonstrate that 30S subunits containing the mutation 726G had an altered binding affinity for mRNA by comparison to the wild type. In addition, expression of the mutant ribosomes in vivo resulted in exclusive suppression of the UGA nonsense codon. This effect was supported by in vitro studies that showed the mutant ribosomes to have an altered binding affinity for Release Factor-2.
Prescott
C D
CD
Max-Planck-Institut für Molekulare Genetik, Abt. Wittmann, Berlin, FRG.
Göringer
H U
HU
D001483:Base Sequence; D003062:Codon; D003720:Densitometry; D004926:Escherichia coli / Q000235:genetics; D015964:Gene Expression Regulation, Bacterial; D008969:Molecular Sequence Data; D009154:Mutation; D010454:Peptide Termination Factors / Q000378:metabolism; D014176:Protein Biosynthesis; D012333:RNA, Messenger / Q000378:metabolism*; D012336:RNA, Ribosomal, 16S / Q000235:genetics*; D012270:Ribosomes / Q000378:metabolism; D014170:Transformation, Genetic
D003062:Codon; D010454:Peptide Termination Factors; D012333:RNA, Messenger; D012336:RNA, Ribosomal, 16S; C041460:peptide chain termination release factor 2