BAIT
RRP5
L000003232, YMR229C
RNA binding protein involved in synthesis of both 18S and 5.8S rRNAs; component of both the ribosomal small subunit (SSU) processosome and the 90S preribosome; acts as part of a Mak21p-Noc2p-Rrp5p module that associates with nascent pre-rRNA during transcription and has a role in bigenesis of the large ribosomal subunit; has binding preference for single stranded tracts of U's; relocalizes from nucleolus to nucleus upon DNA replication stress
GO Process (5)
GO Function (2)
GO Component (3)
Gene Ontology Biological Process
- endonucleolytic cleavage in 5'-ETS of tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [IMP]
- endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [IMP]
- endonucleolytic cleavage in ITS1 upstream of 5.8S rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [IMP]
- endonucleolytic cleavage to generate mature 5'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA) [IMP]
- maturation of SSU-rRNA [IDA]
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Saccharomyces cerevisiae (S288c)
PREY
RIX7
putative AAA family ATPase RIX7, YLL034C
Putative ATPase of the AAA family; required for export of pre-ribosomal large subunits from the nucleus; distributed between the nucleolus, nucleoplasm, and nuclear periphery depending on growth conditions
GO Process (2)
GO Function (1)
GO Component (3)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Saccharomyces cerevisiae (S288c)
Affinity Capture-MS
An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and the associated interaction partner is identified by mass spectrometric methods.
Publication
Rrp5p, Noc1p and Noc2p form a protein module which is part of early large ribosomal subunit precursors in S. cerevisiae.
Eukaryotic ribosome biogenesis requires more than 150 auxiliary proteins, which transiently interact with pre-ribosomal particles. Previous studies suggest that several of these biogenesis factors function together as modules. Using a heterologous expression system, we show that the large ribosomal subunit (LSU) biogenesis factor Noc1p of Saccharomyces cerevisiae can simultaneously interact with the LSU biogenesis factor Noc2p and Rrp5p, a factor ... [more]
Nucleic Acids Res. Jan. 01, 2013; 41(2);1191-1210 [Pubmed: 23209026]
Throughput
- Low Throughput
Curated By
- BioGRID