A base pair between tRNA and 23S rRNA in the peptidyl transferase centre of the ribosome

Article Abstract:

The first specific base-base, tRNA-rRNA interaction has been observed between the tRNA conserved CCA terminal and the 235 rRNA sequences in the peptidyl transferase P site. Observations through selective mutations of the G2252 and G2253 235 rRNA sites and wildtype or mutant aminoacyl-CCA oligonucleotide analogs show a Watson-Crick base pairing between the 235 G2252 site and the C74 tRNA site. This pairing may enable the peptidyl t RNA accepter end to be properly positioned for the elongation phase of protein synthesis.

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Ribosomal peptidyl transferase can withstand mutations at the putative catalytic nucleotide

Article Abstract:

Research is presented describing peptide bond formation in protein synthesis, and how mutations at the putative catalytic nucleotide can be withstood by the ribosomal peptidyl transferase. Alterations in the putative catalytic residues do not have a major affect on peptidyl transfer, and the ribosome properly positions protein systhesis substrates to promote transpeptidation.

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Structural basis for the interaction of antibiotics with the peptidyl transferase centre in eubacteria

Article Abstract:

Research is presented describing antibiotic drug binding and the role of ribosome function in creating antibiotic interactions protein synthesis sites.

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