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

RPL26B

ribosomal 60S subunit protein L26B, L24, YL33, L33B, L26B, L000004462, YGR034W
Ribosomal 60S subunit protein L26B; 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; RPL26B has a paralog, RPL26A, 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)

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
RPL26B RPL26A
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.

High6BioGRID
3601457
RPL26B RPL26A
Dosage Rescue
Dosage Rescue

A genetic interaction is inferred when over expression or increased dosage of one gene rescues the lethality or growth defect of a strain that is mutated or deleted for another gene.

Low-BioGRID
2543956
RPL26B RPL26A
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-0.1228BioGRID
381996
RPL26A RPL26B
Phenotypic Enhancement
Phenotypic Enhancement

A genetic interaction is inferred when mutation or overexpression of one gene results in enhancement of any phenotype (other than lethality/growth defect) associated with mutation or over expression of another gene.

Low-BioGRID
674837
RPL26A RPL26B
Synthetic Growth Defect
Synthetic Growth Defect

A genetic interaction is inferred when mutations in separate genes, each of which alone causes a minimal phenotype, result in a significant growth defect under a given condition when combined in the same cell.

Low-BioGRID
642668

Curated By

  • BioGRID