BAIT
RPA135
RPA2, RRN2, SRP3, DNA-directed RNA polymerase I core subunit RPA135, A135, L000001674, YPR010C
RNA polymerase I second largest subunit A135
GO Process (2)
GO Function (1)
GO Component (1)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Saccharomyces cerevisiae (S288c)
PREY
BFR2
L000004432, YDR299W
Component of the SSU and 90S preribosomes; involved in pre-18S rRNA processing; binds to U3 snoRNA and Mpp10p; multicopy suppressor of sensitivity to Brefeldin A; expression is induced during lag phase and also by cold shock
GO Process (2)
GO Function (0)
GO Component (3)
Gene Ontology Biological Process
Gene Ontology Cellular Component
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
- High Throughput
Additional Notes
- Growing cells containing Protein A-tagged bait protein were crosslinked using formaldehyde. Chromatin fractions were prepared and the bait proteins were purified using IgG coupled magnetic beads. The co-purified proteins were subjected to comparative MS analysis.
Curated By
- BioGRID