Change search
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • 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
The force-sensing peptide VemP employs extreme compaction and secondary structure formation to induce ribosomal stalling
Stockholm University, Faculty of Science, Department of Biochemistry and Biophysics.
Show others and affiliations
Number of Authors: 8
2017 (English)In: eLIFE, E-ISSN 2050-084X, Vol. 6, e25642Article in journal (Refereed) Published
Abstract [en]

Interaction between the nascent polypeptide chain and the ribosomal exit tunnel can modulate the rate of translation and induce translational arrest to regulate expression of downstream genes. The ribosomal tunnel also provides a protected environment for initial protein folding events. Here, we present a 2.9 angstrom cryo-electron microscopy structure of a ribosome stalled during translation of the extremely compacted VemP nascent chain. The nascent chain forms two a-helices connected by an a-turn and a loop, enabling a total of 37 amino acids to be observed within the first 50-55 angstrom of the exit tunnel. The structure reveals how a-helix formation directly within the peptidyltransferase center of the ribosome interferes with aminoacyl-tRNA accommodation, suggesting that during canonical translation, a major role of the exit tunnel is to prevent excessive secondary structure formation that can interfere with the peptidyltransferase activity of the ribosome.

Place, publisher, year, edition, pages
2017. Vol. 6, e25642
National Category
Biological Sciences
Identifiers
URN: urn:nbn:se:su:diva-144810DOI: 10.7554/eLife.25642ISI: 000402309300001OAI: oai:DiVA.org:su-144810DiVA: diva2:1121587
Available from: 2017-07-12 Created: 2017-07-12 Last updated: 2017-07-12Bibliographically approved

Open Access in DiVA

No full text

Other links

Publisher's full text

Search in DiVA

By author/editor
Hedman, Rickardvon Heijne, Gunnar
By organisation
Department of Biochemistry and BiophysicsScience for Life Laboratory (SciLifeLab)
In the same journal
eLIFE
Biological Sciences

Search outside of DiVA

GoogleGoogle Scholar

Altmetric score

Total: 2 hits
CiteExportLink to record
Permanent link

Direct link
Cite
Citation style
  • apa
  • harvard1
  • ieee
  • modern-language-association-8th-edition
  • 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