4GMN

Structural basis of Rpl5 recognition by Syo1

Summary for 4GMN

• Entry DOI: 10.2210/pdb4gmn/pdb
• Descriptor: 60S ribosomal protein l5-like protein, Putative uncharacterized protein (2 entities in total)
• Functional Keywords: arm, heat, solenoid, linear motif, nuclear transport, chaperone, ribosome assembly, rpl11, kap104, rna binding protein
• Biological source: Chaetomium thermophilum; More
• Total number of polymer chains: 2
• Total formula weight: 80782.17

Authors

Bange, G.,Sinning, I. (deposition date: 2012-08-16, release date: 2012-10-31, Last modification date: 2024-02-28)

Primary citation

Kressler, D.,Bange, G.,Ogawa, Y.,Stjepanovic, G.,Bradatsch, B.,Pratte, D.,Amlacher, S.,Strauss, D.,Yoneda, Y.,Katahira, J.,Sinning, I.,Hurt, E.
Synchronizing nuclear import of ribosomal proteins with ribosome assembly.
Science, 338:666-671, 2012

PubMed Abstract: Ribosomal proteins are synthesized in the cytoplasm, before nuclear import and assembly with ribosomal RNA (rRNA). Little is known about coordination of nucleocytoplasmic transport with ribosome assembly. Here, we identify a transport adaptor, symportin 1 (Syo1), that facilitates synchronized coimport of the two 5S-rRNA binding proteins Rpl5 and Rpl11. In vitro studies revealed that Syo1 concomitantly binds Rpl5-Rpl11 and furthermore recruits the import receptor Kap104. The Syo1-Rpl5-Rpl11 import complex is released from Kap104 by RanGTP and can be directly transferred onto the 5S rRNA. Syo1 can shuttle back to the cytoplasm by interaction with phenylalanine-glycine nucleoporins. X-ray crystallography uncovered how the α-solenoid symportin accommodates the Rpl5 amino terminus, normally bound to 5S rRNA, in an extended groove. Symportin-mediated coimport of Rpl5-Rpl11 could ensure coordinated and stoichiometric incorporation of these proteins into pre-60S ribosomes.

PubMed: 23118189
DOI: 10.1126/science.1226960

Experimental method

X-RAY DIFFRACTION (2.95 Å)