ArticleJournal of the American Chemical Society2019
Expanding the Scope of Protein Synthesis Using Modified Ribosomes.
Article in Journal of the American Chemical Society, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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23 citing papers in PubMed, 40 citations in OpenAlex.
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- Elongation Factor P Modulates the Incorporation of Structurally Diverse Noncanonical Amino Acids intoJournal of the American Chemical Society · 2023Article
- Computationally-guided design and selection of high performing ribosomal active site mutants.Nucleic acids research · 2022Article
- Three-dimensional structure-guided evolution of a ribosome with tethered subunits.Nature chemical biology · 2022Article
- Ribosome selectivity and nascent chain context in modulating the incorporation of fluorescent non-canonical amino acid into proteins.Scientific reports · 2022Article
- Reconstruction of the rRNA Sequences of LUCA, with Bioinformatic Implication of the Local Similarities Shared by Them.Biology · 2022Article
- Local Conformational Constraint of Firefly Luciferase Can Affect the Energy of Bioluminescence and Enzyme Stability.CCS chemistry · 2022Article
- Making Sense of "Nonsense" and More: Challenges and Opportunities in the Genetic Code Expansion, in the World of tRNA Modifications.International journal of molecular sciences · 2022Review
- Facilitated synthesis of proteins containing modified dipeptides.Bioorganic & medicinal chemistry · 2021Article
- Posttranslational chemical installation of azoles into translated peptides.Nature communications · 2021Article
- Expression and Clinical Significance of MPS-1 in Hepatocellular Carcinoma.International journal of general medicine · 2021Article
- Mechanistic studies of non-canonical amino acid mutagenesis.Methods in enzymology · 2021Article
- Deciphering protein post-translational modifications using chemical biology tools.Nature reviews. Chemistry · 2020Review
- Protein synthesis with conformationally constrained cyclic dipeptides.Bioorganic & medicinal chemistry · 2020Article
- Ribosome-mediated polymerization of long chain carbon and cyclic amino acids into peptides in vitro.Nature communications · 2020Article
- Mutational characterization and mapping of the 70S ribosome active site.Nucleic acids research · 2020Article
- Strategies for in vitro engineering of the translation machinery.Nucleic acids research · 2020Review
- Single enzyme RT-PCR of full-length ribosomal RNA.Synthetic biology (Oxford, England) · 2020Article
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2 authors at 1 institution in 1 country.
Funding
Abstract
The ribosome produces all of the proteins and many of the peptides present in cells. As a macromolecular complex composed of both RNAs and proteins, it employs a constituent RNA to catalyze the formation of peptide bonds rapidly and with high fidelity. Thus, the ribosome can be argued to represent the key link between the RNA World, in which RNAs were the primary catalysts, and present biological systems in which protein catalysts predominate. In spite of the well-known phylogenetic conservation of rRNAs through evolutionary history, rRNAs can be altered readily when placed under suitable pressure, e.g. in the presence of antibiotics which bind to functionally critical regions of rRNAs. While the structures of rRNAs have been altered intentionally for decades to enable the study of their role(s) in the mechanism of peptide bond formation, it is remarkable that the purposeful alteration of rRNA structure to enable the elaboration of proteins and peptides containing noncanonical amino acids has occurred only recently. In this Perspective, we summarize the history of rRNA modifications, and demonstrate how the intentional modification of 23S rRNA in regions critical for peptide bond formation now enables the direct ribosomal incorporation of d-amino acids, β-amino acids, dipeptides and dipeptidomimetic analogues of the normal proteinogenic l-α-amino acids. While proteins containing metabolically important functional groups such as carbohydrates and phosphate groups are normally elaborated by the post-translational modification of nascent polypeptides, the use of modified ribosomes to produce such polymers directly is also discussed. Finally, we describe the elaboration of such modified proteins both in vitro and in bacterial cells, and suggest how such novel biomaterials may be exploited in future studies.
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