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Structure of the pre-60S ribosomal subunit with nuclear export factor Arx1 bound at the exit tunnel

Preribosomal particles evolve in the nucleus through transient interaction with biogenesis factors before export to the cytoplasm. Here, we report the architecture of the late pre-60S particle, purified from Saccharomyces cerevisiae, through Arx1, a nuclear export factor with structural homology to...

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Hauptverfasser: Bradatsch, Bettina (VerfasserIn) , Gnädig, Marén (VerfasserIn) , Hurt, Ed (VerfasserIn)
Dokumenttyp: Article (Journal)
Sprache:Englisch
Veröffentlicht: 2012
In: Nature structural & molecular biology
Year: 2012, Jahrgang: 19, Heft: 12, Pages: 1234-1241
ISSN:1545-9985
DOI:10.1038/nsmb.2438
Online-Zugang:Verlag, Volltext: http://dx.doi.org/10.1038/nsmb.2438
Verlag, Volltext: https://www.nature.com/articles/nsmb.2438
Volltext
Verfasserangaben:Bettina Bradatsch, Christoph Leidig, Sander Granneman, Marén Gnädig, David Tollervey, Bettina Böttcher, Roland Beckmann & Ed Hurt
Beschreibung
Zusammenfassung:Preribosomal particles evolve in the nucleus through transient interaction with biogenesis factors before export to the cytoplasm. Here, we report the architecture of the late pre-60S particle, purified from Saccharomyces cerevisiae, through Arx1, a nuclear export factor with structural homology to methionine aminopeptidases, or its binding partner Alb1. Cryo-EM reconstruction of the Arx1 particle at 11.9-Å resolution reveals regions of extra density on the pre-60S particle attributed to associated biogenesis factors, confirming the immature state of the nascent subunit. One of these densities could be unambiguously assigned to Arx1. Immunoelectron microscopy and UV cross-linking localize Arx1 close to the ribosomal exit tunnel, in direct contact with ES27, a highly dynamic eukaryotic rRNA expansion segment. The binding of Arx1 at the exit tunnel may position this export factor to prevent premature recruitment of ribosome-associated factors active during translation.
Beschreibung:Published online 11 November 2012
Gesehen am 11.06.2018
Beschreibung:Online Resource
ISSN:1545-9985
DOI:10.1038/nsmb.2438

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