3J2I

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

Summary for 3J2I

• Entry DOI: 10.2210/pdb3j2i/pdb
• Related: 3IZF
• EMDB information: 5513
• Descriptor: Eukaryotic translation initiation factor 6, Proliferation-associated protein 2G4 (2 entities in total)
• Functional Keywords: ribosome, pre-ribosome, cryo-em, ribosomal protein, signaling protein
• Biological source: Saccharomyces cerevisiae (yeast); More
• Total number of polymer chains: 2
• Total formula weight: 70328.48

Authors

Bradatsch, B.,Leidig, C.,Granneman, S.,Gnaedig, M.,Tollervey, D.,Boettcher, B.,Beckmann, R.,Hurt, E. (deposition date: 2012-10-04, release date: 2012-11-07, Last modification date: 2024-02-21)

Primary citation

Bradatsch, B.,Leidig, C.,Granneman, S.,Gnadig, M.,Tollervey, D.,Bottcher, B.,Beckmann, R.,Hurt, E.
Structure of the pre-60S ribosomal subunit with nuclear export factor Arx1 bound at the exit tunnel.
Nat.Struct.Mol.Biol., 19:1234-1241, 2012

PubMed Abstract: 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.

PubMed: 23142978
DOI: 10.1038/nsmb.2438

Experimental method

ELECTRON MICROSCOPY (11.9 Å)