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
SSZ1
PDR13, L000004029, YHR064C
Hsp70 protein that interacts with Zuo1p (a DnaJ homolog); interacts with Zuo1p to form a ribosome-associated complex that binds the ribosome via the Zuo1p subunit; also involved in pleiotropic drug resistance via sequential activation of PDR1 and PDR5; binds ATP
GO Process (4)
GO Function (1)
GO Component (2)
Gene Ontology Biological Process
Gene Ontology Molecular Function
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.
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