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AARS Online: a collaborative database on the structure, function, and evolution of the aminoacyl-tRNA synthetases
Open accessPreprint — published as 10.1002/iub.2911
Abstract
The aminoacyl-tRNA synthetases (aaRS) are a large group of enzymes that implement the genetic code in all known biological systems. They attach amino acids to their cognate tRNAs, moonlight in various non-translational activities, and are linked to many genetic disorders. The aaRS have a subtle ontology characterized by structural and functional idiosyncrasies that vary from organism to organism, and protein to protein. Across the tree of life, the twenty-two coded amino acids are handled by sixteen evolutionary Families of Class I aaRS and twenty-one Families of Class II aaRS. We introduce AARS Online, an interactive Wikipedia-like tool curated by an international consortium of field experts. This platform systematizes existing knowledge about the aaRS by showcasing a taxonomically diverse selection of aaRS sequences and structures. Through its graphical user interface, AARS Online facilitates a seamless exploration between protein sequence and structure, providing a friendly introduction to the material for non-experts and a useful resource for experts. Curated multiple sequence alignments can be extracted for downstream analyses. Accessible at www.aars.online , AARS Online is a free resource to delve into the world of the aaRS.
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Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764
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Research works printed but not linked: 132
- 10.1261/rna.071720.119 · DOI
- 10.1073/pnas.0504682102 · DOI
- 10.1073/pnas.1110889108 · DOI
- 10.1146/annurev.genom.9.081307.164204 · DOI
- 2013, Essential nontranslational functions of tRNA synthetases, Nature chemical biology, 9, 145, 10.1038/nchembio.1158 · DOI
- J. J. Perona and I. Gruic-Sovulj , “Synthetic and editing mechanisms of aminoacyl-tRNA synthetases,” Aminoacyl-tRNA synthetases in biology and medicine, pp. 1–41, 2014. · DOI
- 10.1038/nsb777 · DOI
- 10.1126/science.1108329 · DOI
- 2024, Enzymic recognition of amino acids drove the evolution of primordial genetic codes, Nucleic Acids Research, 52, 558, 10.1093/nar/gkad1160 · DOI
- 10.1093/emboj/cdg148 · DOI
- 10.1111/j.1742-4658.2009.07178.x · DOI
- 10.1111/j.1432-1033.1990.tb15401.x · DOI
- 10.1016/j.str.2006.08.007 · DOI
- 10.1074/jbc.M806745200 · DOI
- 10.1128/jb.165.1.88-93.1986 · DOI
- 10.1074/jbc.M109494200 · DOI
- 10.1073/pnas.1932482100 · DOI
- 10.1073/pnas.1936123100 · DOI
- 1989, Identification of a selenocysteyl-tRNASer in mammalian cells that recognizes the nonsense codon, UGA, Journal of Biological Chemistry, 264, 9724, 10.1016/S0021-9258(18)81714-8 · DOI
- 2019, Mitochondrial aminoacyl-tRNA synthetase disorders: An emerging group of developmental disorders of myelination, Journal of Neurodevelopmental Disorders, 11, 1
- 10.1002/humu.23277 · DOI
- A. K. Turvey , G. A. Horvath , and A. R. Cavalcanti , “Aminoacyl-tRNA synthetases in human health and disease,” Frontiers in Physiology, vol. 13, p. 1029218, 2022. · DOI
- 10.1016/j.ymgme.2013.01.010 · DOI
- 2023, Disease models of mitochondrial aminoacyl-tRNA synthetase defects, Journal of Inherited Metabolic Disease, 46, 817, 10.1002/jimd.12652 · DOI
- 10.1093/gbe/evv095 · DOI
- 10.1093/molbev/msl202 · DOI
- 10.1074/jbc.REV118.002955 · DOI
- 10.1016/j.ajhg.2019.01.006 · DOI
- 2020, Human diseases linked to cytoplasmic aminoacyl-tRNA synthetases, The enzymes, 48, 277, 10.1016/bs.enz.2020.06.009 · DOI
- 10.1093/brain/aws070 · DOI
- I. Yoon , U. Kim , J. Choi , and S. Kim , “Disease association and therapeutic routes of aminoacyl-tRNA synthetases,” Trends in Molecular Medicine, 2024. · DOI
- 10.1016/j.molmed.2017.06.002 · DOI
- 2008, Arrangements in the modular evolution of proteins, Trends in bio chemical sciences, 33, 444, 10.1016/j.tibs.2008.05.008 · DOI
- 10.1016/j.sbi.2013.02.012 · DOI
- 2020, The modular nature of protein evolution: Domain rearrangement rates across eukaryotic life, BMC Evolutionary Biology, 20, 1
- 10.1074/jbc.RA118.004276 · DOI
- 10.1016/j.jmb.2011.03.026 · DOI
- 10.1128/jb.177.17.5179-5185.1995 · DOI
- 10.1105/tpc.10.8.1277 · DOI
- 2020, G: U-independent rna minihelix aminoacylation by nanoarchaeum equitans alanyl-tRNA synthetase: An insight into the evolution of aminoacyl-tRNA synthetases, Journal of molecular evolution, 88, 501, 10.1007/s00239-020-09945-1 · DOI
- L. Klipcan , I. Finarov , N. Moor , and M. G. Safro , “Structural aspects of phenylalanylation and quality control in three major forms of phenylalanyl-tRNA synthetase,” Journal of amino acids, vol. 2010, 2010. · DOI
- 2017, Crystal structures reveal an elusive functional domain of pyrrolysyl-tRNA synthetase, Nature chemical biology, 13, 1261, 10.1038/nchembio.2497 · DOI
- 10.1016/S0968-0004(01)01932-6 · DOI
- 10.1128/MMBR.67.4.550-573.2003 · DOI
- 10.1021/bi301180x · DOI
- C. W. Carter , A. Popinga , R. Bouckaert , and P. R. Wills , “Multidimensional Phylogenetic Metrics Identify Class I Aminoacyl-tRNA Synthetase Evolutionary Mosaicity and Inter-modular Coupling,” International Journal of Molecular Sciences, vol. 23, no. 3, p. 1520, 2022. · DOI
- 10.1038/nature08612 · DOI
- 10.1038/nature06454 · DOI
- 2020, Trans-editing by aminoacyl-tRNA synthetase-like editing domains, The Enzymes, 48, 69, 10.1016/bs.enz.2020.07.002 · DOI
- M. Guo and X.-L. Yang , “Architecture and metamorphosis,” Aminoacyl-tRNA Synthetases in Biology and Medicine, pp. 89–118, 2014. · DOI
- 10.1101/gr.9.8.689 · DOI · Paper page
- 10.1016/S0969-2126(97)00260-8 · DOI
- 10.1093/nar/gkz1064 · DOI
- 10.1074/jbc.M116.730382 · DOI
- 10.1038/nature21031 · DOI · Paper page
- 10.1016/j.jmb.2004.11.060 · DOI
- 10.1016/bs.enz.2020.08.001 · DOI
- 2021, The roots of genetic coding in aminoacyl-tRNA synthetase duality, Annual review of biochemistry, 90, 349, 10.1146/annurev-biochem-071620-021218 · DOI
- 2022, The origin of genetic code and translation in the framework of current concepts on the origin of life, Biochemistry (Moscow, 87, 150, 10.1134/S0006297922020079 · DOI
- 10.1007/BF01582025 · DOI
- 2014, The Rodin-Ohno hypothesis that two enzyme superfamilies descended from one ancestral gene: an unlikely scenario for the origins of translation that will not be dismissed, Biology Direct, 9, 1
- S. Kauffman and N. Lehman , “Mixed Anhydrides at the Intersection Between Peptide and RNA Autocatalytic Sets: Evolution of Biological Coding,” Journal of the Royal Society Interface, 2023. · DOI
- J. J. Hobson , Z. Li , H. Hu , and C. W. Carter Jr , “A Leucyl-tRNA Synthetase Urzyme: Authenticity of tRNA Synthetase Catalytic Activities and Promiscuous Phosphorylation of Leucyl-5’ AMP,” International Journal of Molecular Sciences, vol. 23, no. 8, p. 4229, 2022. · DOI
- 10.1074/jbc.M110.198929 · DOI
- 2023, Domain acquisition by class i aminoacyl-tRNA synthetase urzymes coordinated the catalytic functions of hvgh and kmsks motifs, Nucleic Acids Research, 51, 8070, 10.1093/nar/gkad590 · DOI
- S. K. Patra et al., “Genomic database furnishes a spontaneous example of a functional class ii glycyl-tRNA synthetase urzyme,” bioRxiv, pp. 2024–01, 2024. · DOI
- K. Onodera et al., “Amino acid activation analysis of primitive aminoacyl-tRNA synthetases encoded by both strands of a single gene using the malachite green assay,” BioSystems, vol. 208, p. 104481, 2021. · DOI
- T. Tang , H. Hu , J. Douglas , and C. Carter Jr ., “Primordial aminoacyl-tRNA synthetases preferred tRNA minihelix substrates over full-length tRNA,” In review, 2024. · DOI
- 10.1038/337478a0 · DOI
- 10.1016/S0092-8674(05)80002-9 · DOI
- 10.1074/jbc.274.11.6835 · DOI
- 10.1002/iub.146 · DOI · Paper page
- J. T.-F. Wong , S.-K. Ng , W.-K. Mat , T. Hu , and H. Xue , “Coevolution theory of the genetic code at age forty: Pathway to translation and synthetic life,” Life, vol. 6, no. 1, p. 12, 2016. · DOI · Paper page
- 10.1126/science.7530860 · DOI
- 10.1038/381442a0 · DOI
- 10.1098/rstb.2011.0137 · DOI
- 10.1002/pro.4379 · DOI · Paper page
- 2024, AlphaFold predictions are valuable hypotheses and accelerate but do not replace experimental structure determination, Nature Methods, 21, 110, 10.1038/s41592-023-02087-4 · DOI · Paper page
- 10.1093/emboj/21.11.2778 · DOI
- B. Chen et al., “Inhibitory mechanism of reveromycin a at the tRNA binding site of a class i synthetase,” Nature communications, vol. 12, no. 1, p. 1616, 2021. · DOI
- 10.1126/science.1142189 · DOI
- 10.1016/S0022-2836(03)00917-3 · DOI
- 10.1016/S0092-8674(00)00182-3 · DOI
- 10.1016/S0969-2126(98)00046-X · DOI
- 10.1093/emboj/cdg053 · DOI
- 10.1016/j.jmb.2006.06.054 · DOI
- S. Chung et al., “Regulation of brca1 stability through the tandem ubx domains of isoleucyl-tRNA synthetase 1,” Nature communications, vol. 13, no. 1, p. 6732, 2022. · DOI
- 10.1093/nar/gkq605 · DOI
- 10.1107/S090744490101215X · DOI
- 10.1128/JVI.01107-07 · DOI
- 10.1093/emboj/17.18.5438 · DOI
- 1995, Crystal structure of glycyl-tRNA synthetase from Thermus thermophilus, The EMBO Journal, 14, 4156, 10.1002/j.1460-2075.1995.tb00089.x · DOI
- 10.1016/j.febslet.2007.05.046 · DOI
- 10.1073/pnas.0437911100 · DOI
- 10.1038/sj.emboj.7600811 · DOI
- 10.1038/sj.emboj.7601129 · DOI
- 10.1016/S0022-2836(03)00719-8 · DOI
- 2006, Structural basis of the water-assisted asparagine recognition by asparaginyl-tRNA synthetase, Journal of molecular biology, 360, 329, 10.1016/j.jmb.2006.04.068 · DOI
- 10.1093/emboj/18.22.6532 · DOI
- 10.1006/jmbi.2000.3791 · DOI
- 10.1093/emboj/17.17.5227 · DOI
- 10.1093/jb/mvp014 · DOI
- 10.1016/j.str.2010.01.002 · DOI
- 10.1002/pro.549 · DOI
- 10.1016/j.str.2008.03.020 · DOI
- 10.1002/j.1460-2075.1995.tb00088.x · DOI
- 10.1073/pnas.0611504104 · DOI
- 10.1073/pnas.0704769104 · DOI
- 2022, ColabFold: Making protein folding accessible to all, Nature methods, 19, 679, 10.1038/s41592-022-01488-1 · DOI · Paper page
- 1983, Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features, Biopolymers: Original Research on Biomolecules, 22, 2577, 10.1002/bip.360221211 · DOI · Paper page
- 10.1093/nar/gkq1105 · DOI
- 10.1038/srep01636 · DOI
- 10.1093/bioinformatics/btr432 · DOI
- 2003, Multiple sequence alignment using ClustalW and ClustalX, Current protocols in bioinformatics, 1, 2
- 10.1093/nar/gkz438 · DOI
- 2019, BEAST 2.5: An advanced software platform for Bayesian evolutionary analysis, PLoS computational biology, 15, e1006650, 10.1371/journal.pcbi.1006650 · DOI · Paper page
- 2021, Adaptive dating and fast proposals: Revisiting the phylogenetic relaxed clock model, PLoS computational biology, 17, e1008322, 10.1371/journal.pcbi.1008322 · DOI
- 2020, OBAMA: OBAMA for Bayesian amino-acid model averaging, PeerJ, 8, e9460, 10.7717/peerj.9460 · DOI
- R. R. Bouckaert , “An efficient coalescent epoch model for bayesian phylogenetic inference,” Systematic Biology , p. sya c015, 2022, doi: DOI:10.1093/sysbio/syac015. · DOI
- L. Berling , J. Klawitter , R. Bouckaert , D. Xie , A. Gavryushkin , and A. Drummond , “A tractable tree distribution parameterized by clade probabilities and its application to bayesian phylogenetic point estimation,” bioRxiv, pp. 2024–02, 2024. · DOI
- A. Rambaut , A. J. Drummond , D. Xie , G. Baele , and M. A. Suchard , “Posterior summarization in Bayesian phylogenetics using tracer 1.7,” Systematic biology, vol. 67, no. 5, p. 901, 2018. · DOI · Paper page
- 10.1093/oxfordjournals.molbev.a003851 · DOI · Paper page
- 10.1093/molbev/msn067 · DOI · Paper page
- 10.1016/j.jmb.2004.11.034 · DOI
- 10.1093/nar/gkad007) · DOI
- 10.1038/347203a0 · DOI
- 10.1093/nar/29.1.288 · DOI
- 10.1093/nar/gkw1182 · DOI
- 10.1128/MR.56.1.229-264.1992 · DOI
- 10.1016/0305-0491(93)90122-L · DOI
- S. Placzek et al., “BRENDA in 2017: New perspectives and new tools in brenda,” Nucleic acids research, p. gkw952, 2016. · DOI
- 2024, Common evolutionary origins of the bacterial glycyl tRNA synthetase and alanyl tRNA synthetase, Protein Science, 33, e4844, 10.1002/pro.4844 · DOI
Metadata
- Authors
- Douglas, J., Cui, H., Perona, J. J., Vargas-Rodriguez, O., Tyynismaa, H., Alvarez Carreño, C., Ling, J., Ribas-de-Pouplana, L., Yang, X.-L., Ibba, M., Becker, H., Fischer, F., Sissler, M., Carter, C. W., & Wills, P. R.
- Affiliations
- University of Auckland (NZ)
- University of Toronto (CA)
- Portland State University (US)
- University of Helsinki (FI)
- University of Maryland, College Park (US)
- Scripps Research Institute (US)
- Chapman University (US)
- Génétique Moléculaire Génomique Microbiologie (FR)
- University of North Carolina at Chapel Hill (US)
- Corresponding author
- Douglas, Jordan
- ORCID
- Venue
- IUBMB Life
- Publisher
- openRxiv
- Published
- 2024-05-15
- Volume
- 76
- Issue
- 12
- Pages
- 1091-1105
- ISSN
- 1521-6543 (ISSN-L)
- PMC
- PMC11580382
- OpenAlex
- W4402375721
- Cited by
- 19
- References
- 1
- Citations by year
- 2026: 6 · 2025: 11 · 2024: 2
- FWCI
- 2.56
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- cc-by
- Locations
- IUBMB Life (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- HAL (submittedVersion, other-oa)
- Chapman University Digital Commons (Chapman University) (submittedVersion, cc-by)
- PDXScholar (Portland State University) (submittedVersion, cc-by)
- Työväentutkimus Vuosikirja (submittedVersion)
- Funders
- Alfred P. Sloan Foundation (g-2021-16944)
- Royal Society
- University of Auckland
- Academy of Finland
- Canadian Institutes of Health Research
- Natural Sciences and Engineering Research Council of Canada
- National Institute of General Medical Sciences (R35GM136213, R35GM139627)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA and protein synthesis mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Phylogenetic Studies
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA modifications and cancer
- Keywords
- aminoacyl-tRNA synthetase, protein databases, genetic code, aminoacylation, moonlighting enzymes, protein evolution, multiple sequence alignment, protein structure
- MeSH terms
- Amino Acid Sequence, Amino Acyl-tRNA Synthetases, Animals, Humans, User-Computer Interface, Evolution, Molecular, Internet, Databases, Protein
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