BAIT

RPS27A

ribosomal 40S subunit protein S27A, S27e, rp61, YS20, S27A, L000002712, YKL156W
Protein component of the small (40S) ribosomal subunit; homologous to mammalian ribosomal protein S27, no bacterial homolog; RPS27A has a paralog, RPS27B, that arose from the whole genome duplication; protein abundance increases in response to DNA replication stress
GO Process (3)
GO Function (1)
GO Component (2)
Saccharomyces cerevisiae (S288c)
PREY

RCO1

YMR075W
Essential component of the Rpd3S histone deacetylase complex; interacts with Eaf3p
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

Tsr4 and Nap1, two novel members of the ribosomal protein chaperOME.

Roessler I, Embacher J, Pillet B, Murat G, Liesinger L, Hafner J, Unterluggauer JJ, Birner-Gruenberger R, Kressler D, Pertschy B

Dedicated chaperones protect newly synthesized ribosomal proteins (r-proteins) from aggregation and accompany them on their way to assembly into nascent ribosomes. Currently, only nine of the ?80 eukaryotic r-proteins are known to be guarded by such chaperones. In search of new dedicated r-protein chaperones, we performed a tandem-affinity purification based screen and looked for factors co-enriched with individual small subunit ... [more]

Nucleic Acids Res. Dec. 26, 2018; 47(13);6984-7002 [Pubmed: 31062022]

Throughput

  • High Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
RCO1 RPS27A
Negative Genetic
Negative Genetic

Mutations/deletions in separate genes, each of which alone causes a minimal phenotype, but when combined in the same cell results in a more severe fitness defect or lethality under a given condition. This term is reserved for high or low throughput studies with scores.

High-0.2227BioGRID
404606

Curated By

  • BioGRID