Structural insight into the role of the ribosomal tunnel in cellular regulation. (Articolo in rivista)

Type
Label
  • Structural insight into the role of the ribosomal tunnel in cellular regulation. (Articolo in rivista) (literal)
Anno
  • 2003-01-01T00:00:00+01:00 (literal)
Alternative label
  • Berisio, Rita; Schluenzen, Frank; Harms, Joerg; Bashan, Anat; Auerbach, Tamar; Baram, David; Yonath, Ada. (2003)
    Structural insight into the role of the ribosomal tunnel in cellular regulation.
    in Nature structural biology
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Berisio, Rita; Schluenzen, Frank; Harms, Joerg; Bashan, Anat; Auerbach, Tamar; Baram, David; Yonath, Ada. (literal)
Pagina inizio
  • 366 (literal)
Pagina fine
  • 370 (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#numeroVolume
  • 10 (literal)
Rivista
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#descrizioneSinteticaDelProdotto
  • Articolo su rivista scientica che chiarisce a livello atomico alcuni requisiti per la funzione di antibiotici (literal)
Note
  • ISI Web of Science (WOS) (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
  • Istituto di Biostrutture e Bioimmagini CNR Napoli Max-Planck-Research Unit for Ribosomal Structure, Hamburg, Germany (literal)
Titolo
  • Structural insight into the role of the ribosomal tunnel in cellular regulation. (literal)
Abstract
  • Nascent proteins emerge out of ribosomes through an exit tunnel, which was assumed to be a firmly built passive path. Recent biochem. results, however, indicate that the tunnel plays an active role in sequence-specific gating of nascent chains and in responding to cellular signals. Consistently, modulation of the tunnel shape, caused by the binding of the semi-synthetic macrolide troleandomycin to the large ribosomal subunit from Deinococcus radiodurans, was revealed crystallog. The results provide insights into the tunnel dynamics at high resoln. Here we show that, in addn. to the typical steric blockage of the ribosomal tunnel by macrolides, troleandomycin induces a conformational rearrangement in a wall constituent, protein L22, flipping the tip of its highly conserved b-hairpin across the tunnel. On the basis of mutations that alleviate elongation arrest, the tunnel motion could be correlated with sequence discrimination and gating, suggesting that specific arrest motifs within nascent chain sequences may induce a similar gating mechanism. (literal)
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