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Träfflista för sökning "WFRF:(Beckmann Roland) ;pers:(Hedman Rickard)"

Sökning: WFRF:(Beckmann Roland) > Hedman Rickard

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1.
  • Nilsson, Ola B., et al. (författare)
  • Cotranslational Protein Folding inside the Ribosome Exit Tunnel
  • 2015
  • Ingår i: Cell Reports. - : Elsevier BV. - 2211-1247. ; 12:10, s. 1533-1540
  • Tidskriftsartikel (refereegranskat)abstract
    • At what point during translation do proteins fold? It is well established that proteins can fold cotranslationally outside the ribosome exit tunnel, whereas studies of folding inside the exit tunnel have so far detected only the formation of helical secondary structure and collapsed or partially structured folding intermediates. Here, using a combination of co-translational nascent chain force measurements, inter-subunit fluorescence resonance energy transfer studies on single translating ribosomes, molecular dynamics simulations, and cryoelectron microscopy, we show that a small zinc-finger domain protein can fold deep inside the vestibule of the ribosome exit tunnel. Thus, for small protein domains, the ribosome itself can provide the kind of sheltered folding environment that chaperones provide for larger proteins.
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2.
  • Su, Ting, et al. (författare)
  • The force-sensing peptide VemP employs extreme compaction and secondary structure formation to induce ribosomal stalling
  • 2017
  • Ingår i: eLIFE. - 2050-084X. ; 6
  • Tidskriftsartikel (refereegranskat)abstract
    • 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.
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