Logo: to the web site of Uppsala University

uu.sePublications from Uppsala University
Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf
Cryo-EM visualization of the ribosome in termination complex with apo-RF3 and RF1
Columbia University.
Columbia University.
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.
Show others and affiliations
2013 (English)In: eLife, ISSN 2050-084X, Vol. 2, p. e00411-Article in journal (Refereed) Published
Abstract [en]

Termination of messenger RNA translation in Bacteria and Archaea is initiated by release factors (RFs) 1 or 2 recognizing a stop codon in the ribosomal A site and releasing the peptide from the P-site transfer RNA. After release, RF-dissociation is facilitated by the G-protein RF3. Structures of ribosomal complexes with RF1 or RF2 alone or with RF3 alone-RF3 bound to a non-hydrolyzable GTP-analog-have been reported. Here, we present the cryo-EM structure of a post-termination ribosome containing both apo-RF3 and RF1. The conformation of RF3 is distinct from those of free RF3•GDP and ribosome-bound RF3•GDP(C/N)P. Furthermore, the conformation of RF1 differs from those observed in RF3-lacking ribosomal complexes. Our study provides structural keys to the mechanism of guanine nucleotide exchange on RF3 and to an L12-mediated ribosomal recruitment of RF3. In conjunction with previous observations, our data provide the foundation to structurally characterize the complete action cycle of the G-protein RF3.

Place, publisher, year, edition, pages
2013. Vol. 2, p. e00411-
National Category
Biological Sciences
Research subject
Molecular Biology
Identifiers
URN: urn:nbn:se:uu:diva-207130DOI: 10.7554/eLife.00411ISI: 000328616200001OAI: oai:DiVA.org:uu-207130DiVA, id: diva2:647266
Available from: 2013-09-11 Created: 2013-09-09 Last updated: 2014-01-17Bibliographically approved

Open Access in DiVA

Pallesen eLIFE(8964 kB)400 downloads
File information
File name FULLTEXT01.pdfFile size 8964 kBChecksum SHA-512
aac4b43d5020ba21196e5c2dd3b97f7cad37b9a7ae438b9f79948728639ce1cf164576251e5cf384036f5f790bd130c07d8b86884d57a6e3e29dc5b2e6bb46f8
Type fulltextMimetype application/pdf

Other links

Publisher's full text

Authority records

Korkmaz, GürkanKoripella, Ravi KiranEhrenberg, MånsSanyal, Suparna Chandra

Search in DiVA

By author/editor
Korkmaz, GürkanKoripella, Ravi KiranEhrenberg, MånsSanyal, Suparna Chandra
By organisation
Structure and Molecular BiologyDepartment of Cell and Molecular Biology
Biological Sciences

Search outside of DiVA

GoogleGoogle Scholar
Total: 400 downloads
The number of downloads is the sum of all downloads of full texts. It may include eg previous versions that are now no longer available

doi
urn-nbn

Altmetric score

doi
urn-nbn
Total: 686 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • ieee
  • modern-language-association
  • vancouver
  • Other style
More styles
Language
  • de-DE
  • en-GB
  • en-US
  • fi-FI
  • nn-NO
  • nn-NB
  • sv-SE
  • Other locale
More languages
Output format
  • html
  • text
  • asciidoc
  • rtf