ArticleProceedings of the National Academy of Sciences of the United States of America2010
Homologs of aminoacyl-tRNA synthetases acylate carrier proteins and provide a link between ribosomal and nonribosomal peptide synthesis.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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25 citing papers in PubMed, 62 citations in OpenAlex.
- Proteome-metabolome profiling of wax gland complex reveals functional changes in honeybee,iScience · 2024Article
- Diversification of aminoacyl-tRNA synthetase activitiesFrontiers in physiology · 2022Review
- Glycine-derived nitronates bifurcate to O-methylation or denitrification in bacteria.Nature chemistry · 2021Article
- Origin of the Genetic Code Is Found at the Transition between a Thioester World of Peptides and the Phosphoester World of Polynucleotides.Life (Basel, Switzerland) · 2019Article
- Self-Referential Encoding on Modules of Anticodon Pairs-Roots of the Biological Flow System.Life (Basel, Switzerland) · 2017Review
- The complex evolutionary history of aminoacyl-tRNA synthetases.Nucleic acids research · 2017Article
- Homocysteine Editing, Thioester Chemistry, Coenzyme A, and the Origin of Coded Peptide Synthesis †.Life (Basel, Switzerland) · 2017Review
- Deep Sequencing of Suppression Subtractive Hybridisation Drought and Recovery Libraries of the Non-model CropFrontiers in plant science · 2017Article
- Aminoacyl-tRNA Synthetases in the Bacterial World.EcoSal Plus · 2016Review
- Discovery Strategies of Bioactive Compounds Synthesized by Nonribosomal Peptide Synthetases and Type-I Polyketide Synthases Derived from Marine Microbiomes.Marine drugs · 2016Review
- Spontaneous mutual ordering of nucleic acids and proteins.Origins of life and evolution of the biosphere : the journal of the International Society for the Study of the Origin of Life · 2014Article
- Origins and emergent evolution of life: the colloid microsphere hypothesis revisited.Origins of life and evolution of the biosphere : the journal of the International Society for the Study of the Origin of Life · 2014Article
- Emergence and evolution.Topics in current chemistry · 2014Review
- RNA function and phosphorus use by photosynthetic organisms.Frontiers in plant science · 2013Review
- Nonproteinogenic amino acid building blocks for nonribosomal peptide and hybrid polyketide scaffolds.Angewandte Chemie (International ed. in English) · 2013Review
- Structural phylogenomics retrodicts the origin of the genetic code and uncovers the evolutionary impact of protein flexibility.PloS one · 2013Article
- Life's Order, Complexity, Organization, and Its Thermodynamic-Holistic Imperatives.Life (Basel, Switzerland) · 2012Article
- Molecular insights into the biosynthesis of guadinomine: a type III secretion system inhibitor.Journal of the American Chemical Society · 2012Article
- Elevated cytokinin content in ipt transgenic creeping bentgrass promotes drought tolerance through regulating metabolite accumulation.Journal of experimental botany · 2012Article
- The phylogenomic roots of modern biochemistry: origins of proteins, cofactors and protein biosynthesis.Journal of molecular evolution · 2012Article
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Aminoacyl-tRNA synthetases (aaRSs) are ancient and evolutionary conserved enzymes catalyzing the formation of aminoacyl-tRNAs, that are used as substrates for ribosomal protein biosynthesis. In addition to full length aaRS genes, genomes of many organisms are sprinkled with truncated genes encoding single-domain aaRS-like proteins, which often have relinquished their canonical role in genetic code translation. We have identified the genes for putative seryl-tRNA synthetase homologs widespread in bacterial genomes and characterized three of them biochemically and structurally. The proteins encoded are homologous to the catalytic domain of highly diverged, atypical seryl-tRNA synthetases (aSerRSs) found only in methanogenic archaea and are deprived of the tRNA-binding domain. Remarkably, in comparison to SerRSs, aSerRS homologs display different and relaxed amino acid specificity. aSerRS homologs lack canonical tRNA aminoacylating activity and instead transfer activated amino acid to phosphopantetheine prosthetic group of putative carrier proteins, whose genes were identified in the genomic surroundings of aSerRS homologs. Detailed kinetic analysis confirmed that aSerRS homologs aminoacylate these carrier proteins efficiently and specifically. Accordingly, aSerRS homologs were renamed amino acid:[carrier protein] ligases (AMP forming). The enzymatic activity of aSerRS homologs is reminiscent of adenylation domains in nonribosomal peptide synthesis, and thus they represent an intriguing link between programmable ribosomal protein biosynthesis and template-independent nonribosomal peptide synthesis.
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