BAIT

MTR4

DOB1, ATP-dependent RNA helicase MTR4, L000004110, YJL050W
ATP-dependent 3'-5' RNA helicase of the DExD/H family; involved in nuclear RNA processing and degradation both as a component of TRAMP complex and in TRAMP-independent processes; TRAMP unwinds RNA duplexes, with Mtr4p unwinding activity stimulated by Pap2p/Air2p but not dependent on ongoing polyadenylation; contains an arch domain, with two coiled-coil arms/stalks and a globular fist/KOW domain, which has RNA binding activity and is required for 5.8S rRNA processing
Saccharomyces cerevisiae (S288c)
PREY

RLP7

RPL7, L000001647, YNL002C
Nucleolar protein similar to large ribosomal subunit L7 proteins; constituent of 66S pre-ribosomal particles; plays an essential role in processing of precursors to the large ribosomal subunit RNAs; binds junction of ITS2 and ITS2-proximal stem between the 3' end of 5.8S rRNA and the 5' end of 25S rRNA
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

The Exosome Is Recruited to RNA Substrates through Specific Adaptor Proteins.

Thoms M, Thomson E, Bassler J, Gnaedig M, Griesel S, Hurt E

The exosome regulates the processing, degradation, and surveillance of a plethora of RNA species. However, little is known about how the exosome recognizes and is recruited to its diverse substrates. We report the identification of adaptor proteins that recruit the exosome-associated helicase, Mtr4, to unique RNA substrates. Nop53, the yeast homolog of the tumor suppressor PICT1, targets Mtr4 to pre-ribosomal ... [more]

Cell Aug. 27, 2015; 162(5);1029-38 [Pubmed: 26317469]

Throughput

  • High Throughput

Related interactions

InteractionExperimental Evidence CodeDatasetThroughputScoreCurated ByNotes
MTR4 RLP7
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-0.1944BioGRID
1938909

Curated By

  • BioGRID