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Frameshift mutations can be suppressed by a variety of differently acting external suppressors. The +1 frameshift mutation  hisC3072 , which has an extra G in a run of Gs, is corrected by the external suppressor mutation  sufF44 . We have shown that  sufF44  and five additional allelic suppressor mutations are located in the gene  argU  coding for the minor tRNA Arg  mnm 5 UCU  and alter the secondary and/or tertiary structure of this tRNA. The C61U, G53A, and C32U mutations influence the stability, whereas the C56U, C61U, G53A, and G39A mutations decrease the arginylation of tRNA Arg  mnm 5 UCU . The T-10C mutant has a base substitution in the -10 consensus sequence of the  argU  promoter that reduces threefold the synthesis of tRNA Arg  mnm 5 UCU  . The lower amount of tRNA Arg  mnm 5 UCU  or impaired arginylation, either independently or in conjunction, results in inefficient reading of the cognate AGA codon that, in turn, induces frameshifts. According to the sequence of the peptide produced from the suppressed -GGG-GAA-AGA- frameshift site, the frameshifting tRNA in the  argU  mutants is tRNA mnm 5 s 2 UUC  Glu , which decodes the GAA codon located upstream of the AGA arginine codon, and not the mutated tRNA Arg  mnm 5 UCU . We propose that an inefficient decoding of the AGA codon by a defective tRNA Arg  mnm 5 UCU  stalls the ribosome at the A-site codon allowing the wild-type form of peptidyl- tRNA mnm 5 s 2 UUC  Glu  to slip forward 1 nucleotide and thereby re-establish the ribosome in the 0-frame. Similar frame-shifting events could be the main cause of various phenotypes associated with environmental or genetically induced changes in the levels of aminoacylated tRNA.

A reduced level of charged tRNAArgmnm5UCU triggers the wild-type peptidyl-tRNA to frameshift

A reduced level of charged tRNA^Arg_mnm⁵UCU triggers the wild-type peptidyl-tRNA to frameshift