BAIT

RPS9A

ribosomal 40S subunit protein S9A, rp21, YS11, S9A, S4, S13, L000004474, YPL081W
Protein component of the small (40S) ribosomal subunit; homologous to mammalian ribosomal protein S9 and bacterial S4; RPS9A has a paralog, RPS9B, that arose from the whole genome duplication
Saccharomyces cerevisiae (S288c)
PREY

MRPL3

mitochondrial 54S ribosomal protein YmL3, YmL3, L000002683, YMR024W
Mitochondrial ribosomal protein of the large subunit; located in close proximity to the polypeptide exit channel of the ribosome; mutations in human homolog MRPL44 cause childhood cardiomyopathy; human MRPL44 deficiency results in inefficient assembly of the mitochondrial ribosome, and in tissue-specific respiratory chain deficiency, manifesting as either Complex I+Complex IV or Complex IV deficiency, depending on a cell type
GO Process (1)
GO Function (1)
GO Component (2)

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