ArticleProceedings of the National Academy of Sciences of the United States of America2003
RNA recognition by designed peptide fusion creates "artificial" tRNA synthetase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 11 citations in OpenAlex.
- Aminoacyl-tRNA Synthetases in the Bacterial World.EcoSal Plus · 2016Review
- Motif-programmed artificial protein induces apoptosis in several cancer cells by disrupting mitochondria.Cancer science · 2008Article
- Motif programming: a microgene-based method for creating synthetic proteins containing multiple functional motifs.Nucleic acids research · 2007Article
- The role of peptide motifs in the evolution of a protein network.Nucleic acids research · 2007Article
- Leucyl-tRNA synthetase from the ancestral bacterium Aquifex aeolicus contains relics of synthetase evolution.The EMBO journal · 2005Article
- Single amino acid changes in AspRS reveal alternative routes for expanding its tRNA repertoire in vivo.Nucleic acids research · 2004Article
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Authors and funding
3 authors at 2 institutions in 2 countries.
Funding
Abstract
The genetic code was established through aminoacylations of RNA substrates that emerged as tRNAs. The 20 aminoacyl-tRNA synthetases (one for each amino acid) are ancient proteins, the active-site domain of which catalyzes formation of an aminoacyl adenylate that subsequently reacts with the 3' end of bound tRNA. Binding of tRNA depends on idiosyncratic (to the particular synthetase) domains and motifs that are fused to or inserted into the conserved active-site domain. Here we take the domain for synthesis of alanyl adenylate and fuse it to "artificial" peptide sequences (28 aa) that were shown previously to bind to the acceptor arm of tRNAAla. Certain fusions confer aminoacylation activity on tRNAAla and on hairpin microhelices modeled after its acceptor stem. Aminoacylation was sensitive to the presence of a specific G:U base pair known to be a major determinant of tRNAAla identity. Aminoacylation efficiency and specificity also depended on the specific peptide sequence. The results demonstrate that barriers to RNA-specific aminoacylations are low and can be achieved by relatively simple peptide fusions. They also suggest a paradigm for rationally designed specific aminoacylations based on peptide fusions.
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