{"entity": "researcher", "timestamp": "2026-09-27T17:02:31.919Z", "family": "Forster", "given": "Anthony C", "initials": "AC", "orcid": "0000-0002-5844-6916", "affiliations": ["Department of Cell and Molecular Biology, Uppsala University, Husargatan 3, Box 596, Uppsala, 75124, Sweden. a.forster@icm.uu.se."], "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/researcher/b1f2f2d4993a405ba214bc40392707de.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/researcher/b1f2f2d4993a405ba214bc40392707de"}}, "publications": [{"entity": "publication", "iuid": "b31b708709ee4714b6b7609562042733", "links": {"self": {"href": "https://publications-affiliated.scilifelab.se/publication/b31b708709ee4714b6b7609562042733.json"}, "display": {"href": "https://publications-affiliated.scilifelab.se/publication/b31b708709ee4714b6b7609562042733"}}, "title": "Translational roles of the C75 2'OH in an in vitro tRNA transcript at the ribosomal A, P and E sites.", "authors": [{"family": "Wang", "given": "Jinfan", "initials": "J", "orcid": "0000-0003-4170-9289", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/cd6d26d25ad7494c86673c8f9281c8b8.json"}}, {"family": "Forster", "given": "Anthony C", "initials": "AC", "orcid": "0000-0002-5844-6916", "researcher": {"href": "https://publications-affiliated.scilifelab.se/researcher/b1f2f2d4993a405ba214bc40392707de.json"}}], "type": "journal article", "published": "2017-07-27", "journal": {"title": "Sci Rep", "issn": "2045-2322", "volume": "7", "issue": "1", "pages": "6709", "issn-l": "2045-2322"}, "abstract": "Aminoacyl-tRNAs containing a deoxy substitution in the penultimate nucleotide (C75 2'OH \u2192 2'H) have been widely used in translation for incorporation of unnatural amino acids (AAs). However, this supposedly innocuous modification surprisingly increased peptidyl-tRNAAlaugc drop off in biochemical assays of successive incorporations. Here we predict the function of this tRNA 2'OH in the ribosomal A, P and E sites using recent co-crystal structures of ribosomes and tRNA substrates and test these structure-function models by systematic kinetics analyses. Unexpectedly, the C75 2'H did not affect A- to P-site translocation nor peptidyl donor activity of tRNAAlaugc. Rather, the peptidyl acceptor activity of the A-site Ala-tRNAAlaugc and the translocation of the P-site deacylated tRNAAlaugc to the E site were impeded. Delivery by EF-Tu was not significantly affected. This broadens our view of the roles of 2'OH groups in tRNAs in translation.", "doi": "10.1038/s41598-017-06991-6", "pmid": "28751745", "labels": [], "xrefs": [{"db": "pmc", "key": "PMC5532260"}, {"db": "pii", "key": "10.1038/s41598-017-06991-6"}], "notes": [], "created": "2026-09-23T13:34:00.357Z", "modified": "2026-09-23T13:34:00.484Z"}]}