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Cryo-EM shows stages of initial codon selection on the ribosome by aa-tRNA in ternary complex with GTP and the GTPase-deficient EF-Tu(H84A)
VIB VUB Ctr Struct Biol, Brussels, Belgium;Columbia Univ, Dept Biochem & Mol Biophys, New York, NY 10027 USA;Vrije Univ Brussel, Struct Biol Brussels, Brussels, Belgium.ORCID iD: 0000-0002-2527-2657
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology. Columbia Univ, Dept Biochem & Mol Biophys, New York, NY 10027 USA.
Osaka Univ, Inst Prot Res, Lab Prot Synth & Express, Osaka, Japan;Columbia Univ, Dept Biochem & Mol Biophys, New York, NY 10027 USA.ORCID iD: 0000-0002-9846-2822
Uppsala University, Disciplinary Domain of Science and Technology, Biology, Department of Cell and Molecular Biology, Molecular Biology.
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2018 (English)In: Nucleic Acids Research, ISSN 0305-1048, E-ISSN 1362-4962, Vol. 46, no 11, p. 5861-5874Article in journal (Refereed) Published
Abstract [en]

The GTPase EF-Tu in ternary complex with GTP and aminoacyl-tRNA (aa-tRNA) promotes rapid and accurate delivery of cognate aa-tRNAs to the ribosomal A site. Here we used cryo-EM to study the molecular origins of the accuracy of ribosome-aided recognition of a cognate ternary complex and the accuracy-amplifying role of themonitoring bases A1492, A1493 and G530 of the 16S rRNA. We used the GTPase-deficient EF-Tu variant H84A with native GTP, rather than non-cleavable GTP analogues, to trap a near-cognate ternary complex in high-resolution ribosomal complexes of varying codon-recognition accuracy. We found that ribosome complexes trapped by GTPase-deficicent ternary complex due to the presence of EF-TuH84A or non-cleavable GTP analogues have very similar structures. We further discuss speed and accuracy of initial aa-tRNA selection in terms of conformational changes of aa-tRNA and stepwise activation of the monitoring bases at the decoding center of the ribosome.

Place, publisher, year, edition, pages
OXFORD UNIV PRESS , 2018. Vol. 46, no 11, p. 5861-5874
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Biochemistry and Molecular Biology
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URN: urn:nbn:se:uu:diva-361119DOI: 10.1093/nar/gky346ISI: 000438362400042PubMedID: 29733411OAI: oai:DiVA.org:uu-361119DiVA, id: diva2:1249903
Funder
Swedish Research Council, 2013-8778Swedish Research Council, 2014-4423Swedish Research Council, 2016-06264Swedish Research Council, 2017-00230Knut and Alice Wallenberg Foundation, KAW 2011.0081NIH (National Institute of Health), R01 GM29169Available from: 2018-09-20 Created: 2018-09-20 Last updated: 2018-09-20Bibliographically approved

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Zhang, JingjiMandava, Chandra SekharSanyal, SuparnaEhrenberg, Måns

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