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

RPA34

CST21, DNA-directed RNA polymerase I subunit RPA34, A34.5, L000004132, L000003000, S000029123, YJL148W
RNA polymerase I subunit A34.5; essential for nucleolar assembly and for high polymerase loading rate; nucleolar localization depends on Rpa49p
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.

Hierlmeier T, Merl J, Sauert M, Perez-Fernandez J, Schultz P, Bruckmann A, Hamperl S, Ohmayer U, Rachel R, Jacob A, Hergert K, Deutzmann R, Griesenbeck J, Hurt E, Milkereit P, Bassler J, Tschochner H

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.

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
RPA34 RPA135
Affinity Capture-MS
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.

High-BioGRID
-
RPA34 RPA135
Affinity Capture-MS
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.

High-BioGRID
-
RPA34 RPA135
Affinity Capture-MS
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.

High10BioGRID
3610779
RPA135 RPA34
Cross-Linking-MS (XL-MS)
Cross-Linking-MS (XL-MS)

An interaction is detected between two proteins using chemically reactive or photo-activatable cross-linking reagents that covalently link amino acids in close proximity, followed by mass spectrometry analysis to identify the linked peptides (reviewed in PMID 37406423, 37104977). Experiments may be carried with live cells or cell lysates in which all proteins are expressed at endogenous levels (e.g. PMID 34349018, 35235311) or with recombinant proteins (e.g., PMID 28537071).

High-BioGRID
3730522
RPA34 RPA135
Synthetic Lethality
Synthetic Lethality

A genetic interaction is inferred when mutations or deletions in separate genes, each of which alone causes a minimal phenotype, result in lethality when combined in the same cell under a given condition.

Low-BioGRID
262938

Curated By

  • BioGRID