Luis Cruz-Vera

Ribosome stalling and peptidyl-tRNA drop-off during translational delay at AGA codons.

Features of ribosome-peptidyl-tRNA interactions essential for tryptophan induction of tna operon expression.

Changes produced by bound tryptophan in the ribosome peptidyl transferase center in response to TnaC, a nascent leader peptide.

Excess of charged tRNALys maintains low levels of peptidyl-tRNA hydrolase in pth(Ts) mutants at a non-permissive temperature.

Ribosome recycling factor and release factor 3 action promotes TnaC-peptidyl-tRNA Dropoff and relieves ribosome stalling during tryptophan induction of tna operon expression in Escherichia coli.

Ribosomal features essential for tna operon induction: tryptophan binding at the peptidyl transferase center.

Efficient expression of gene variants that harbour AGA codons next to the initiation codon.

Physiological effects of anti-TRAP protein activity and tRNA(Trp) charging on trp operon expression in Bacillus subtilis.

Conserved residues Asp16 and Pro24 of TnaC-tRNAPro participate in tryptophan induction of Tna operon expression.

23S rRNA nucleotides in the peptidyl transferase center are essential for tryptophanase operon induction.

Tryptophan inhibits Proteus vulgaris TnaC leader peptide elongation, activating tna operon expression.

Nascent polypeptide sequences that influence ribosome function.

Crucial elements that maintain the interactions between the regulatory TnaC peptide and the ribosome exit tunnel responsible for Trp inhibition of ribosome function.

Peptidyl-tRNA hydrolase screening combined with molecular docking reveals the antibiotic potential of Syzygium johnsonii bark extract.