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Translational roles of the C75 2 ' OH in an in vitro tRNA transcript at the ribosomal A, P and E sites
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Structure and Molecular Biology.
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Structure and Molecular Biology.
2017 (English)In: Scientific Reports, ISSN 2045-2322, E-ISSN 2045-2322, Vol. 7, 6709Article in journal (Refereed) Published
Abstract [en]

Aminoacyl-tRNAs containing a deoxy substitution in the penultimate nucleotide (C75 2'OH -> 2'H) have been widely used in translation for incorporation of unnatural amino acids (AAs). However, this supposedly innocuous modification surprisingly increased peptidyl-tRNA(ugc)(Ala) 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 tRNA(ugc)(Ala). Rather, the peptidyl acceptor activity of the A-site Ala-tRNA(ugc)(Ala) and the translocation of the P-site deacylated tRNA(ugc)(Ala) 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.

Place, publisher, year, edition, pages
NATURE PUBLISHING GROUP , 2017. Vol. 7, 6709
National Category
Cell and Molecular Biology
Identifiers
URN: urn:nbn:se:uu:diva-332839DOI: 10.1038/s41598-017-06991-6ISI: 000406366000067PubMedID: 28751745OAI: oai:DiVA.org:uu-332839DiVA: diva2:1155746
Funder
Swedish Research Council, 2011-5787, 2016-1
Available from: 2017-11-09 Created: 2017-11-09 Last updated: 2017-11-09Bibliographically approved

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