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Adding α,α-disubstituted and β-linked monomers to the genetic code of an organism

The genetic code of living cells has been reprogrammed to enable the site-specific incorporation of hundreds of non-canonical amino acids into proteins, and the encoded synthesis of non-canonical polymers and macrocyclic peptides and depsipeptides1–3. Current methods for engineering orthogonal aminoacyl-tRNA synthetases to acylate new monomers, as required for the expansion and reprogramming of the genetic code, rely on translational readouts and therefore require the monomers to be ribosomal substrates4–6. Orthogonal synthetases cannot be evolved to acylate orthogonal tRNAs with non-canonical monomers (ncMs) that are poor ribosomal substrates, and ribosomes cannot be evolved to polymerize ncMs that cannot be acylated onto orthogonal tRNAs—this co-dependence creates an evolutionary deadlock that has essentially restricted the scope of translation in living cells to α-l-amino acids and closely related hydroxy acids. Here we break this deadlock by developing tRNA d ....

El Yacoubi , Melo Czekster , Acta Crystallogr , Acids Res , Protein Sci , Peptide Sci , Illumina Paired End ,

Frontiers | Functional characterization of VirB/VirD4 and Icm/Dot type IV secretion systems from the plant-pathogenic bacterium Xanthomonas euvesicatoria

Frontiers | Functional characterization of VirB/VirD4 and Icm/Dot type IV secretion systems from the plant-pathogenic bacterium Xanthomonas euvesicatoria
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Permskiy Kray , Orlovskaya Oblast , United States , Gomez Valero , Xanthomonas Vir , Xanthomonas Hrp , Atpase Hrc , Deutsche Forschungsgemeinschaft , Atpase Vir , Agrobacterium Virb Vir , Atpases Dot , El Yacoubi , Atpases Vir , Legionella Ral , Sigma Aldrich , Nh Plenum , Ic Organization , A Organization , Xanthomonas Vird , Early Cal Wonder , Vilber Fusion , Golden Gate Compatible , Golden Gate , Thermo Scientific , Supplementary Material , Med Abstract ,