{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Guo M"],"funding":["NIGMS NIH HHS"],"pagination":["808-12"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC2799227"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["462(7274)"],"pubmed_abstract":["Mistranslation arising from confusion of serine for alanine by alanyl-tRNA synthetases (AlaRSs) has profound functional consequences. Throughout evolution, two editing checkpoints prevent disease-causing mistranslation from confusing glycine or serine for alanine at the active site of AlaRS. In both bacteria and mice, Ser poses a bigger challenge than Gly. One checkpoint is the AlaRS editing centre, and the other is from widely distributed AlaXps-free-standing, genome-encoded editing proteins that clear Ser-tRNA(Ala). The paradox of misincorporating both a smaller (glycine) and a larger (serine) amino acid suggests a deep conflict for nature-designed AlaRS. Here we show the chemical basis for this conflict. Nine crystal structures, together with kinetic and mutational analysis, provided sn"],"journal":["Nature"],"pubmed_title":["Paradox of mistranslation of serine for alanine caused by AlaRS recognition dilemma."],"pmcid":["PMC2799227"],"funding_grant_id":["GM 15539","R01 GM015539"],"pubmed_authors":["Guo M","Beebe K","Shapiro R","Schimmel P","Chong YE","Yang XL"],"additional_accession":[]},"is_claimable":false,"name":"Paradox of mistranslation of serine for alanine caused by AlaRS recognition dilemma.","description":"Mistranslation arising from confusion of serine for alanine by alanyl-tRNA synthetases (AlaRSs) has profound functional consequences. Throughout evolution, two editing checkpoints prevent disease-causing mistranslation from confusing glycine or serine for alanine at the active site of AlaRS. In both bacteria and mice, Ser poses a bigger challenge than Gly. One checkpoint is the AlaRS editing centre, and the other is from widely distributed AlaXps-free-standing, genome-encoded editing proteins that clear Ser-tRNA(Ala). The paradox of misincorporating both a smaller (glycine) and a larger (serine) amino acid suggests a deep conflict for nature-designed AlaRS. Here we show the chemical basis for this conflict. Nine crystal structures, together with kinetic and mutational analysis, provided sn","dates":{"release":"2009-01-01T00:00:00Z","publication":"2009 Dec","modification":"2026-05-02T05:43:21.79Z","creation":"2019-03-26T22:34:02Z"},"accession":"S-EPMC2799227","cross_references":{"pubmed":["20010690"],"doi":["10.1038/nature08612"]}}