BAIT

RPS13

RPS13B, RPS13C, ribosomal 40S subunit protein S13, YS15, S27a, S15, S13, L000002900, L000002655, YDR064W
Protein component of the small (40S) ribosomal subunit; homologous to mammalian ribosomal protein S13 and bacterial S15
Saccharomyces cerevisiae (S288c)
PREY

DBP9

L000004249, YLR276C
DEAD-box protein required for 27S rRNA processing; exhibits DNA, RNA and DNA/RNA helicase activities; ATPase activity shows preference for DNA over RNA; DNA helicase activity abolished by mutation in RNA-binding domain
GO Process (1)
GO Function (4)
GO Component (1)

Gene Ontology Biological Process

Gene Ontology Molecular Function

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

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