BAIT

RPL22A

ribosomal 60S subunit protein L22A, L22e, rp4, l1c, YL31, L22A, L000004460, YLR061W
Ribosomal 60S subunit protein L22A; required for the oxidative stress response in yeast; homologous to mammalian ribosomal protein L22, no bacterial homolog; RPL22A has a paralog, RPL22B, that arose from the whole genome duplication
GO Process (1)
GO Function (1)
GO Component (1)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

Saccharomyces cerevisiae (S288c)
PREY

RPL38

ribosomal 60S subunit protein L38, L38e, L38, L000004468, YLR325C
Ribosomal 60S subunit protein L38; homologous to mammalian ribosomal protein L38, no bacterial homolog
GO Process (1)
GO Function (1)
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

Mechanism of completion of peptidyltransferase centre assembly in eukaryotes.

Kargas V, Castro-Hartmann P, Escudero-Urquijo N, Dent K, Hilcenko C, Sailer C, Zisser G, Marques-Carvalho MJ, Pellegrino S, Wawiorka L, Freund SM, Wagstaff JL, Andreeva A, Faille A, Chen E, Stengel F, Bergler H, Warren AJ

During their final maturation in the cytoplasm, pre-60S ribosomal particles are converted to translation-competent large ribosomal subunits. Here, we present the mechanism of peptidyltransferase centre (PTC) completion that explains how integration of the last ribosomal proteins is coupled to release of the nuclear export adaptor Nmd3. Single-particle cryo-EM reveals that eL40 recruitment stabilizes helix 89 to form the uL16 binding ... [more]

Elife May. 22, 2019; 8(); [Pubmed: 31115337]

Throughput

  • High Throughput

Additional Notes

  • chemical crosslink

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
RPL22A RPL38
Affinity Capture-MS
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.

High5BioGRID
3601092
RPL22A RPL38
Negative Genetic
Negative Genetic

Mutations/deletions in separate genes, each of which alone causes a minimal phenotype, but when combined in the same cell results in a more severe fitness defect or lethality under a given condition. This term is reserved for high or low throughput studies with scores.

High-0.2529BioGRID
397228
RPL22A RPL38
Negative Genetic
Negative Genetic

Mutations/deletions in separate genes, each of which alone causes a minimal phenotype, but when combined in the same cell results in a more severe fitness defect or lethality under a given condition. This term is reserved for high or low throughput studies with scores.

High-0.2402BioGRID
2150078
RPL38 RPL22A
Negative Genetic
Negative Genetic

Mutations/deletions in separate genes, each of which alone causes a minimal phenotype, but when combined in the same cell results in a more severe fitness defect or lethality under a given condition. This term is reserved for high or low throughput studies with scores.

High-0.1988BioGRID
2154218

Curated By

  • BioGRID