Download
e1600379.full.pdf 990,76KB
WeightNameValue
1000 Titel
  • Structural analysis of a signal peptide inside the ribosome tunnel by DNP MAS NMR
1000 Autor/in
  1. Lange, Sascha |
  2. Franks, W. Trent |
  3. Rajagopalan, Nandhakishore |
  4. Döring, Kristina |
  5. Geiger, Michael A. |
  6. Linden, Arne |
  7. van Rossum, Barth-Jan |
  8. Kramer, Günter |
  9. Bukau, Bernd |
  10. Oschkinat, Hartmut |
1000 Erscheinungsjahr 2016
1000 Art der Datei
1000 Publikationstyp
  1. Artikel |
1000 Online veröffentlicht
  • 2016-08-19
1000 Erschienen in
1000 Quellenangabe
  • 2(8): e1600379
1000 FRL-Sammlung
1000 Copyrightjahr
  • 2016
1000 Lizenz
1000 Verlagsversion
  • http://dx.doi.org/10.1126/sciadv.1600379 |
  • https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4991931/ |
1000 Ergänzendes Material
  • http://advances.sciencemag.org/cgi/content/full/2/8/e1600379/DC1 |
1000 Publikationsstatus
1000 Begutachtungsstatus
1000 Sprache der Publikation
1000 Abstract/Summary
  • Proteins are synthesized in cells by ribosomes and, in parallel, prepared for folding or targeting. While ribosomal protein synthesis is progressing, the nascent chain exposes amino-terminal signal sequences or transmembrane domains that mediate interactions with specific interaction partners, such as the signal recognition particle (SRP), the SecA–adenosine triphosphatase, or the trigger factor. These binding events can set the course for folding in the cytoplasm and translocation across or insertion into membranes. A distinction of the respective pathways depends largely on the hydrophobicity of the recognition sequence. Hydrophobic transmembrane domains stabilize SRP binding, whereas less hydrophobic signal sequences, typical for periplasmic and outer membrane proteins, stimulate SecA binding and disfavor SRP interactions. In this context, the formation of helical structures of signal peptides within the ribosome was considered to be an important factor. We applied dynamic nuclear polarization magic-angle spinning nuclear magnetic resonance to investigate the conformational states of the disulfide oxidoreductase A (DsbA) signal peptide stalled within the exit tunnel of the ribosome. Our results suggest that the nascent chain comprising the DsbA signal sequence adopts an extended structure in the ribosome with only minor populations of helical structure.
1000 Sacherschließung
lokal signal peptide
lokal dynamic nuclear polarisation
lokal MAS NMR
lokal co-translational folding
lokal ribosome
lokal Protein structure
1000 Fachgruppe
  1. Medizin |
1000 Fächerklassifikation (DDC)
1000 Liste der Beteiligten
  1. https://frl.publisso.de/adhoc/creator/TGFuZ2UsIFNhc2NoYQ==|https://frl.publisso.de/adhoc/creator/RnJhbmtzLCBXLiBUcmVudA==|https://frl.publisso.de/adhoc/creator/UmFqYWdvcGFsYW4sIE5hbmRoYWtpc2hvcmU=|https://frl.publisso.de/adhoc/creator/RMO2cmluZywgS3Jpc3RpbmE=|https://frl.publisso.de/adhoc/creator/R2VpZ2VyLCBNaWNoYWVsIEEu|https://frl.publisso.de/adhoc/creator/TGluZGVuLCBBcm5l|https://frl.publisso.de/adhoc/creator/dmFuIFJvc3N1bSwgQmFydGgtSmFu|https://frl.publisso.de/adhoc/creator/S3JhbWVyLCBHw7xudGVy|https://frl.publisso.de/adhoc/creator/QnVrYXUsIEJlcm5k|https://frl.publisso.de/adhoc/creator/T3NjaGtpbmF0LCBIYXJ0bXV0
1000 Label
1000 Förderer
  1. Deutsche Forschungsgemeinschaft |
  2. European project iNEXT |
1000 Fördernummer
  1. SFB 740
  2. -
1000 Förderprogramm
  1. -
  2. -
1000 Dateien
1000 Förderung
  1. 1000 joinedFunding-child
    1000 Förderer Deutsche Forschungsgemeinschaft |
    1000 Förderprogramm -
    1000 Fördernummer SFB 740
  2. 1000 joinedFunding-child
    1000 Förderer European project iNEXT |
    1000 Förderprogramm -
    1000 Fördernummer -
1000 Objektart article
1000 Beschrieben durch
1000 @id frl:6403613.rdf
1000 Erstellt am 2017-07-31T15:35:07.034+0200
1000 Erstellt von 22
1000 beschreibt frl:6403613
1000 Bearbeitet von 218
1000 Zuletzt bearbeitet Thu Jan 30 23:07:14 CET 2020
1000 Objekt bearb. Thu Nov 22 12:41:56 CET 2018
1000 Vgl. frl:6403613
1000 Oai Id
  1. oai:frl.publisso.de:frl:6403613 |
1000 Sichtbarkeit Metadaten public
1000 Sichtbarkeit Daten public
1000 Gegenstand von

View source