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

RPS7A

RPS30, ribosomal 40S subunit protein S7A, S7e, rp30, S7A, L000003300, YOR096W
Protein component of the small (40S) ribosomal subunit; interacts with Kti11p; deletion causes hypersensitivity to zymocin; homologous to mammalian ribosomal protein S7, no bacterial homolog; RPS7A has a paralog, RPS7B, that arose from the whole genome duplication
GO Process (4)
GO Function (1)
GO Component (3)

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

Curated By

  • BioGRID