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

Autor: Bettina Bradatsch, Bettina Böttcher, Sander Granneman, David Tollervey, Ed Hurt, Christoph Leidig, Roland Beckmann, Marén Gnädig
Jazyk: angličtina
Rok vydání: 2012
Předmět:
Zdroj: Nature structural & molecular biology
Bradatsch, B, Leidig, C, Granneman, S, Gnädig, M, Tollervey, D, Böttcher, B, Beckmann, R & Hurt, E 2012, ' Structure of the pre-60S ribosomal subunit with nuclear export factor Arx1 bound at the exit tunnel ', Nature Structural & Molecular Biology . https://doi.org/10.1038/nsmb.2438
ISSN: 1545-9985
1545-9993
DOI: 10.1038/nsmb.2438
Popis: Pre-ribosomal 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-electron microscopy reconstruction of the Arx1-particle at 11.9 Å resolution reveals regions of extra densities 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. Immuno-electron 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.
Databáze: OpenAIRE