2MBY

NMR Structure of Rrp7 C-terminal Domain

Summary for 2MBY

• Entry DOI: 10.2210/pdb2mby/pdb
• Related: 4M5D
• NMR Information: BMRB: 19416
• Descriptor: Ribosomal RNA-processing protein 7 (1 entity in total)
• Functional Keywords: 90s preribosome, nucleolus, rna binding protein
• Biological source: Saccharomyces cerevisiae (yeast)
• Cellular location: Nucleus, nucleolus: P25368
• Total number of polymer chains: 1
• Total formula weight: 5732.64

Authors

Lin, J.,Feng, Y.,Ye, K. (deposition date: 2013-08-08, release date: 2013-09-25, Last modification date: 2024-05-15)

Primary citation

Lin, J.,Lu, J.,Feng, Y.,Sun, M.,Ye, K.
An RNA-Binding Complex Involved in Ribosome Biogenesis Contains a Protein with Homology to tRNA CCA-Adding Enzyme.
Plos Biol., 11:e1001669-e1001669, 2013

PubMed Abstract: A multitude of proteins and small nucleolar RNAs transiently associate with eukaryotic ribosomal RNAs to direct their modification and processing and the assembly of ribosomal proteins. Utp22 and Rrp7, two interacting proteins with no recognizable domain, are components of the 90S preribosome or the small subunit processome that conducts early processing of 18S rRNA. Here, we determine the cocrystal structure of Utp22 and Rrp7 complex at 1.97 Å resolution and the NMR structure of a C-terminal fragment of Rrp7, which is not visible in the crystal structure. The structure reveals that Utp22 surprisingly resembles a dimeric class I tRNA CCA-adding enzyme yet with degenerate active sites, raising an interesting evolutionary connection between tRNA and rRNA processing machineries. Rrp7 binds extensively to Utp22 using a deviant RNA recognition motif and an extended linker. Functional sites on the two proteins were identified by structure-based mutagenesis in yeast. We show that Rrp7 contains a flexible RNA-binding C-terminal tail that is essential for association with preribosomes. RNA-protein crosslinking shows that Rrp7 binds at the central domain of 18S rRNA and shares a neighborhood with two processing H/ACA snoRNAs snR30 and snR10. Depletion of snR30 prevents the stable assembly of Rrp7 into preribosomes. Our results provide insight into the evolutionary origin and functional context of Utp22 and Rrp7.

PubMed: 24130456
DOI: 10.1371/journal.pbio.1001669

Experimental method

SOLUTION NMR