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: | , , |
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| Dokumenttyp: | Article (Journal) |
| Sprache: | Englisch |
| Veröffentlicht: |
2012
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| 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 
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| Verfasserangaben: | Bettina Bradatsch, Christoph Leidig, Sander Granneman, Marén Gnädig, David Tollervey, Bettina Böttcher, Roland Beckmann & Ed Hurt |
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| 520 | |a 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. | ||
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