4WJU

Crystal structure of Rsa4 from Saccharomyces cerevisiae

Summary for 4WJU

• Entry DOI: 10.2210/pdb4wju/pdb
• Related: 4WJS
• Descriptor: Ribosome assembly protein 4, GLYCEROL (2 entities in total)
• Functional Keywords: ribosome biogenesis ribosome assembly, biosynthetic protein
• Biological source: Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast); More
• Cellular location: Nucleus, nucleolus : P25382
• Total number of polymer chains: 2
• Total formula weight: 114305.66

Authors

Holdermann, I.,Bassler, J.,Hurt, E.,Sinning, I. (deposition date: 2014-10-01, release date: 2014-11-19, Last modification date: 2024-01-10)

Primary citation

Baler, J.,Paternoga, H.,Holdermann, I.,Thoms, M.,Granneman, S.,Barrio-Garcia, C.,Nyarko, A.,Stier, G.,Clark, S.A.,Schraivogel, D.,Kallas, M.,Beckmann, R.,Tollervey, D.,Barbar, E.,Sinning, I.,Hurt, E.
A network of assembly factors is involved in remodeling rRNA elements during preribosome maturation.
J.Cell Biol., 207:481-498, 2014

PubMed Abstract: Eukaryotic ribosome biogenesis involves ∼200 assembly factors, but how these contribute to ribosome maturation is poorly understood. Here, we identify a network of factors on the nascent 60S subunit that actively remodels preribosome structure. At its hub is Rsa4, a direct substrate of the force-generating ATPase Rea1. We show that Rsa4 is connected to the central protuberance by binding to Rpl5 and to ribosomal RNA (rRNA) helix 89 of the nascent peptidyl transferase center (PTC) through Nsa2. Importantly, Nsa2 binds to helix 89 before relocation of helix 89 to the PTC. Structure-based mutations of these factors reveal the functional importance of their interactions for ribosome assembly. Thus, Rsa4 is held tightly in the preribosome and can serve as a "distribution box," transmitting remodeling energy from Rea1 into the developing ribosome. We suggest that a relay-like factor network coupled to a mechano-enzyme is strategically positioned to relocate rRNA elements during ribosome maturation.

PubMed: 25404745
DOI: 10.1083/jcb.201408111

Experimental method

X-RAY DIFFRACTION (2.8 Å)