BAIT

RPL26A

ribosomal 60S subunit protein L26A, L24, YL33, L33A, L26A, L000004461, YLR344W
Ribosomal 60S subunit protein L26A; binds to 5.8S rRNA; non-essential even when paralog is also deleted; deletion has minimal affections on ribosome biosynthesis; homologous to mammalian ribosomal protein L26 and bacterial L24; RPL26A has a paralog, RPL26B, that arose from the whole genome duplication
GO Process (1)
GO Function (2)
GO Component (1)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Saccharomyces cerevisiae (S288c)
PREY

UTP23

YOR004W
Component of the small subunit processome; involved in 40S ribosomal subunit biogenesis; interacts with snR30 and is required for dissociation of snR30 from large pre-ribosomal particles; has homology to PINc domain protein Fcf1p, although the PINc domain of Utp23p is not required for function; essential protein
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