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
Kinome Project (Sc)
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)

Gene Ontology Biological Process

Gene Ontology Molecular Function

Gene Ontology Cellular Component

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

Structure of the no-go mRNA decay complex Dom34-Hbs1 bound to a stalled 80S ribosome.

Becker T, Armache JP, Jarasch A, Anger AM, Villa E, Sieber H, Motaal BA, Mielke T, Berninghausen O, Beckmann R

No-go decay (NGD) is a mRNA quality-control mechanism in eukaryotic cells that leads to degradation of mRNAs stalled during translational elongation. The key factors triggering NGD are Dom34 and Hbs1. We used cryo-EM to visualize NGD intermediates resulting from binding of the Dom34-Hbs1 complex to stalled ribosomes. At subnanometer resolution, all domains of Dom34 and Hbs1 were identified, allowing the ... [more]

Nat. Struct. Mol. Biol. Jun. 01, 2011; 18(6);715-20 [Pubmed: 21623367]

Throughput

  • Low Throughput

Additional Notes

  • structures determined by cryo-EM

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
-
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