BAIT

RPS1A

RP10A, ribosomal 40S subunit protein S1A, S1e, S1A, L000001664, YLR441C
Ribosomal protein 10 (rp10) of the small (40S) subunit; homologous to mammalian ribosomal protein S3A, no bacterial homolog; RPS1A has a paralog, RPS1B, that arose from the whole genome duplication
GO Process (2)
GO Function (1)
GO Component (2)
Saccharomyces cerevisiae (S288c)
PREY

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)
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

Curated By

  • BioGRID