The pathway to GTPase activation of elongation factor SelB on the ribosome

Niels Fischer (), Piotr Neumann, Lars V. Bock, Cristina Maracci, Zhe Wang, Alena Paleskava, Andrey L. Konevega, Gunnar F Schröder, Helmut Grubmüller, Ralf Ficner, Marina V. Rodnina and Holger Stark ()
Additional contact information
Niels Fischer: Max Planck Institute for Biophysical Chemistry
Piotr Neumann: Institute for Microbiology and Genetics, GZMB, Georg-August University Göttingen
Lars V. Bock: Max Planck Institute for Biophysical Chemistry
Cristina Maracci: Max Planck Institute for Biophysical Chemistry
Zhe Wang: Institute of Complex Systems (ICS-6)
Alena Paleskava: Max Planck Institute for Biophysical Chemistry
Andrey L. Konevega: Max Planck Institute for Biophysical Chemistry
Gunnar F Schröder: Institute of Complex Systems (ICS-6)
Helmut Grubmüller: Max Planck Institute for Biophysical Chemistry
Ralf Ficner: Institute for Microbiology and Genetics, GZMB, Georg-August University Göttingen
Marina V. Rodnina: Max Planck Institute for Biophysical Chemistry
Holger Stark: Max Planck Institute for Biophysical Chemistry

Nature, 2016, vol. 540, issue 7631, 80-85

Abstract: Abstract In all domains of life, selenocysteine (Sec) is delivered to the ribosome by selenocysteine-specific tRNA (tRNASec) with the help of a specialized translation factor, SelB in bacteria. Sec-tRNASec recodes a UGA stop codon next to a downstream mRNA stem–loop. Here we present the structures of six intermediates on the pathway of UGA recoding in Escherichia coli by single-particle cryo-electron microscopy. The structures explain the specificity of Sec-tRNASec binding by SelB and show large-scale rearrangements of Sec-tRNASec. Upon initial binding of SelB–Sec-tRNASec to the ribosome and codon reading, the 30S subunit adopts an open conformation with Sec-tRNASec covering the sarcin–ricin loop (SRL) on the 50S subunit. Subsequent codon recognition results in a local closure of the decoding site, which moves Sec-tRNASec away from the SRL and triggers a global closure of the 30S subunit shoulder domain. As a consequence, SelB docks on the SRL, activating the GTPase of SelB. These results reveal how codon recognition triggers GTPase activation in translational GTPases.

Date: 2016
References: Add references at CitEc
Citations: View citations in EconPapers (2)

Downloads: (external link)
https://www.nature.com/articles/nature20560 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:540:y:2016:i:7631:d:10.1038_nature20560

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/nature20560

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().