BAIT

DOM34

ribosome dissociation factor DOM34, L000000517, YNL001W
Protein that facilitates ribosomal subunit dissociation; Dom34-Hbs1 complex and Rli1p have roles in dissociating inactive ribosomes to facilitate translation restart, particularly ribosomes stalled in 3' UTRs; required for RNA cleavage in no-go decay, but reports conflict on endonuclease activity; Pelota ortholog; protein abundance increases in response to DNA replication stress; DOM34 has a paralog, YCL001W-B, that arose from the whole genome duplication
Saccharomyces cerevisiae (S288c)
PREY

RPS23A

ribosomal 40S subunit protein S23A, rp37, YS14, S28A, S23A, S12, L000001764, YGR118W
Ribosomal protein 28 (rp28) of the small (40S) ribosomal subunit; required for translational accuracy; homologous to mammalian ribosomal protein S23 and bacterial S12; RPS23A has a paralog, RPS23B, that arose from the whole genome duplication; deletion of both RPS23A and RPS23B is lethal
GO Process (2)
GO Function (1)
GO Component (1)
Saccharomyces cerevisiae (S288c)

Co-crystal Structure

Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.

Publication

Structural insights into ribosomal rescue by Dom34 and Hbs1 at near-atomic resolution.

Hilal T, Yamamoto H, Loerke J, Buerger J, Mielke T, Spahn CM

The surveillance of mRNA translation is imperative for homeostasis. Monitoring the integrity of the message is essential, as the translation of aberrant mRNAs leads to stalling of the translational machinery. During ribosomal rescue, arrested ribosomes are specifically recognized by the conserved eukaryotic proteins Dom34 and Hbs1, to initiate their recycling. Here we solve the structure of Dom34 and Hbs1 bound ... [more]

Nat Commun Dec. 20, 2015; 7();13521 [Pubmed: 27995908]

Throughput

  • Low Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
DOM34 RPS23A
Co-crystal Structure
Co-crystal Structure

Interaction directly demonstrated at the atomic level by X-ray crystallography. Also used for NMR or Electron Microscopy (EM) structures. If there is no obvious bait-hit directionality to the interaction involving 3 or more proteins, then the co-crystallized proteins should be listed as a complex.

Low-BioGRID
553839
RPS23A DOM34
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-0.2382BioGRID
382569
DOM34 RPS23A
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-0.4714BioGRID
2166737
DOM34 RPS23A
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.

High-BioGRID
483834

Curated By

  • BioGRID