Archaeal aminoacyl-tRNA synthetases interact with the ribosome to recycle tRNAs
dc.contributor.author
Godinic-Mikulcic, Vlatka
dc.contributor.author
Jaric, Jelena
dc.contributor.author
Greber, Basil J.
dc.contributor.author
Franke, Vedran
dc.contributor.author
Hodnik, Vesna
dc.contributor.author
Anderluh, Gregor
dc.contributor.author
Ban, Nenad
dc.contributor.author
Weygand-Durasevic, Ivana
dc.date.accessioned
2020-07-07T05:25:04Z
dc.date.available
2017-06-11T09:09:25Z
dc.date.available
2019-04-04T10:35:37Z
dc.date.available
2020-07-07T05:25:04Z
dc.date.issued
2014-04-01
dc.identifier.issn
1362-4962
dc.identifier.issn
0301-5610
dc.identifier.other
10.1093/nar/gku164
en_US
dc.identifier.uri
http://hdl.handle.net/20.500.11850/84809
dc.identifier.doi
10.3929/ethz-b-000084809
dc.description.abstract
Aminoacyl-tRNA synthetases (aaRS) are essential enzymes catalyzing the formation of aminoacyl-tRNAs, the immediate precursors for encoded peptides in ribosomal protein synthesis. Previous studies have suggested a link between tRNA aminoacylation and high-molecular-weight cellular complexes such as the cytoskeleton or ribosomes. However, the structural basis of these interactions and potential mechanistic implications are not well understood. To biochemically characterize these interactions we have used a system of two interacting archaeal aaRSs: an atypical methanogenic-type seryl-tRNA synthetase and an archaeal ArgRS. More specifically, we have shown by thermophoresis and surface plasmon resonance that these two aaRSs bind to the large ribosomal subunit with micromolar affinities. We have identified the L7/L12 stalk and the proteins located near the stalk base as the main sites for aaRS binding. Finally, we have performed a bioinformatics analysis of synonymous codons in the Methanothermobacter thermautotrophicus genome that supports a mechanism in which the deacylated tRNAs may be recharged by aaRSs bound to the ribosome and reused at the next occurrence of a codon encoding the same amino acid. These results suggest a mechanism of tRNA recycling in which aaRSs associate with the L7/L12 stalk region to recapture the tRNAs released from the preceding ribosome in polysomes.
en_US
dc.format
application/pdf
en_US
dc.language.iso
en
en_US
dc.publisher
Oxford University Press
en_US
dc.rights.uri
http://creativecommons.org/licenses/by/3.0/
dc.title
Archaeal aminoacyl-tRNA synthetases interact with the ribosome to recycle tRNAs
en_US
dc.type
Journal Article
dc.rights.license
Creative Commons Attribution 3.0 Unported
dc.date.published
2014-02-24
ethz.journal.title
Nucleic Acids Research
ethz.journal.volume
42
en_US
ethz.journal.issue
8
en_US
ethz.journal.abbreviated
Nucleic Acids Res.
ethz.pages.start
5191
en_US
ethz.pages.end
5201
en_US
ethz.size
11 p.
en_US
ethz.version.deposit
publishedVersion
en_US
ethz.notes
It was possible to publish this article open access thanks to a Swiss National Licence with the publisher
en_US
ethz.identifier.wos
ethz.publication.place
Oxford
en_US
ethz.publication.status
published
en_US
ethz.leitzahl
ETH Zürich::00002 - ETH Zürich::00012 - Lehre und Forschung::00007 - Departemente::02030 - Dep. Biologie / Dep. of Biology::02521 - Inst. f. Molekularbiologie u. Biophysik / Inst. Molecular Biology and Biophysics::03556 - Ban, Nenad / Ban, Nenad
en_US
ethz.leitzahl.certified
ETH Zürich::00002 - ETH Zürich::00012 - Lehre und Forschung::00007 - Departemente::02030 - Dep. Biologie / Dep. of Biology::02521 - Inst. f. Molekularbiologie u. Biophysik / Inst. Molecular Biology and Biophysics::03556 - Ban, Nenad / Ban, Nenad
ethz.date.deposited
2017-06-11T09:10:26Z
ethz.source
ECIT
ethz.identifier.importid
imp593651f3eabd616063
ethz.ecitpid
pub:133760
ethz.eth
yes
en_US
ethz.availability
Open access
en_US
ethz.rosetta.installDate
2017-07-12T17:44:49Z
ethz.rosetta.lastUpdated
2024-02-02T11:21:48Z
ethz.rosetta.versionExported
true
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