Matthias D. Erlacher

TL;DR: The findings suggest that M1A on mRNA, probably because of its disruptive impact on base pairing, leads to translational repression, and is generally avoided by cells, while revealing one case in mitochondria where tight spatiotemporal control over m1A levels was adopted as a potential means of post-transcriptional regulation.

TL;DR: The results suggest a novel mode of gene regulation by nucleotide modifications in bacterial mRNAs, which is consistent with stalling of translation at the modified codon of the bacterial ErmCL mRNA.

TL;DR: It is proposed that the A2451-2'-hydroxyl directly hydrogen bonds to the P-site tRNA-A76 ribose, thus promoting effective peptide bond synthesis and demonstrating that hydrogen donor capability is essential for transpeptidation.

TL;DR: A novel modified nucleoside interference approach was applied to identify functional groups at 9 universally conserved active site residues and the ribose 2'-OH of A2451 was identified as the prime ribosomal group with potential functional importance.

TL;DR: The main finding is that ribosomes carrying a 2′-deoxyribose at A2451 showed a compromised peptidyl transferase activity, which implicates a functional or structural role of the 2-hydroxyl group at A 2451 for transpeptidation.