3JCT

Cryo-em structure of eukaryotic pre-60S ribosomal subunits

This is a non-PDB format compatible entry.

Summary for 3JCT

• Entry DOI: 10.2210/pdb3jct/pdb
• EMDB information: 6615
• Descriptor: 60S ribosomal protein L2-A, 60S ribosomal protein L11-A, Proteasome-interacting protein CIC1, ... (61 entities in total)
• Functional Keywords: pre-60s ribosome, ribosome
• Biological source: Saccharomyces cerevisiae S288c (yeast); More
• Total number of polymer chains: 58
• Total formula weight: 2679630.35

Authors

Wu, S.,Kumcuoglu, B.,Yan, K.G.,Brown, H.,Zhang, Y.X.,Tan, D.,Gamalinda, M.,Yuan, Y.,Li, Z.F.,Jakovljevic, J.,Ma, C.Y.,Lei, J.L.,Dong, M.Q.,Woolford Jr., J.L.,Gao, N. (deposition date: 2016-03-09, release date: 2016-06-01, Last modification date: 2024-03-20)

Primary citation

Wu, S.,Tutuncuoglu, B.,Yan, K.,Brown, H.,Zhang, Y.,Tan, D.,Gamalinda, M.,Yuan, Y.,Li, Z.,Jakovljevic, J.,Ma, C.,Lei, J.,Dong, M.Q.,Woolford, J.L.,Gao, N.
Diverse roles of assembly factors revealed by structures of late nuclear pre-60S ribosomes
Nature, 534:133-137, 2016

PubMed Abstract: Ribosome biogenesis is a highly complex process in eukaryotes, involving temporally and spatially regulated ribosomal protein (r-protein) binding and ribosomal RNA remodelling events in the nucleolus, nucleoplasm and cytoplasm. Hundreds of assembly factors, organized into sequential functional groups, facilitate and guide the maturation process into productive assembly branches in and across different cellular compartments. However, the precise mechanisms by which these assembly factors function are largely unknown. Here we use cryo-electron microscopy to characterize the structures of yeast nucleoplasmic pre-60S particles affinity-purified using the epitope-tagged assembly factor Nog2. Our data pinpoint the locations and determine the structures of over 20 assembly factors, which are enriched in two areas: an arc region extending from the central protuberance to the polypeptide tunnel exit, and the domain including the internal transcribed spacer 2 (ITS2) that separates 5.8S and 25S ribosomal RNAs. In particular, two regulatory GTPases, Nog2 and Nog1, act as hub proteins to interact with multiple, distant assembly factors and functional ribosomal RNA elements, manifesting their critical roles in structural remodelling checkpoints and nuclear export. Moreover, our snapshots of compositionally and structurally different pre-60S intermediates provide essential mechanistic details for three major remodelling events before nuclear export: rotation of the 5S ribonucleoprotein, construction of the active centre and ITS2 removal. The rich structural information in our structures provides a framework to dissect molecular roles of diverse assembly factors in eukaryotic ribosome assembly.

PubMed: 27251291
DOI: 10.1038/nature17942

Experimental method

ELECTRON MICROSCOPY (3.08 Å)