BAIT

LSM1

SPB8, L000004427, YJL124C
Lsm (Like Sm) protein; forms heteroheptameric complex (with Lsm2p, Lsm3p, Lsm4p, Lsm5p, Lsm6p, and Lsm7p) involved in degradation of cytoplasmic mRNAs; also enters the nucleus and positively regulates transcription initiation; unlike most Sm-like proteins, Lsm1p requires both its SM-domain and C-terminal domain for RNA-binding; binds to mRNAs under glucose starvation, most often in the 3' UTR; forms cytoplasmic foci upon DNA replication stress
Saccharomyces cerevisiae (S288c)
PREY

TIF4632

eIF4G2, L000002310, YGL049C
Translation initiation factor eIF4G; subunit of the mRNA cap-binding protein complex (eIF4F) that also contains eIF4E (Cdc33p); associates with the poly(A)-binding protein Pab1p, also interacts with eIF4A (Tif1p); TIF4632 has a paralog, TIF4631, that arose from the whole genome duplication
Saccharomyces cerevisiae (S288c)

Affinity Capture-Western

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 identified by Western blot with a specific polyclonal antibody or second epitope tag. This category is also used if an interacting protein is visualized directly by dye stain or radioactivity. Note that this differs from any co-purification experiment involving affinity capture in that the co-purification experiment involves at least one extra purification step to get rid of potential contaminating proteins.

Publication

Engineered rings of mixed yeast Lsm proteins show differential interactions with translation factors and U-rich RNA.

Sobti M, Cubeddu L, Haynes PA, Mabbutt BC

The Lsm proteins organize as heteroheptameric ring assemblies capable of binding RNA substrates and ancillary protein factors. We have constructed simplified Lsm polyproteins that organize as multimeric ring structures as analogues of the functional Lsm complexes. Polyproteins Lsm[2+3], Lsm[4+1], and Lsm[5+6] incorporate natural sequence extensions as linker peptides between the core Lsm domains. In solution, the recombinant products organize as ... [more]

Biochemistry Mar. 23, 2010; 49(11);2335-45 [Pubmed: 20108977]

Throughput

  • Low Throughput

Curated By

  • BioGRID