BAIT

AIR2

YDL175C
RNA-binding subunit of the TRAMP nuclear RNA surveillance complex; involved in nuclear RNA processing and degradation; involved in TRAMP complex assembly as a bridge between Mtr4p and Trf4p; stimulates the poly(A) polymerase activity of Pap2p in vitro; has 5 zinc knuckle motifs; AIR2 has a paralog, AIR1, that arose from the whole genome duplication; Air2p and Air1p have nonredundant roles in regulation of substrate specificity of the exosome
Saccharomyces cerevisiae (S288c)
PREY

XRN1

DST2, KEM1, RAR5, SEP1, SKI1, chromatin-binding exonuclease XRN1, L000000891, L000001902, YGL173C
Evolutionarily-conserved 5'-3' exonuclease; component of cytoplasmic processing (P) bodies involved in mRNA decay; also enters the nucleus and positively regulates transcription initiation and elongation; plays a role in microtubule-mediated processes, filamentous growth, ribosomal RNA maturation, and telomere maintenance; activated by the scavenger decapping enzyme Dcs1p
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

Substrate specificity of the TRAMP nuclear surveillance complexes.

Delan-Forino C, Spanos C, Rappsilber J, Tollervey D

During nuclear surveillance in yeast, the RNA exosome functions together with the TRAMP complexes. These include the DEAH-box RNA helicase Mtr4 together with an RNA-binding protein (Air1 or Air2) and a poly(A) polymerase (Trf4 or Trf5). To better determine how RNA substrates are targeted, we analyzed protein and RNA interactions for TRAMP components. Mass spectrometry identified three distinct TRAMP complexes ... [more]

Nat Commun Dec. 19, 2019; 11(1);3122 [Pubmed: 32561742]

Throughput

  • Low Throughput

Curated By

  • BioGRID