BAIT

GPD1

DAR1, HOR1, OSG1, OSR5, glycerol-3-phosphate dehydrogenase (NAD(+)) GPD1, L000000722, YDL022W
NAD-dependent glycerol-3-phosphate dehydrogenase; key enzyme of glycerol synthesis, essential for growth under osmotic stress; expression regulated by high-osmolarity glycerol response pathway; protein abundance increases in response to DNA replication stress; constitutively inactivated via phosphorylation by the protein kinases YPK1 and YPK2, dephosphorylation increases catalytic activity; GPD1 has a paralog, GPD2, that arose from the whole genome duplication
GO Process (2)
GO Function (1)
GO Component (3)

Gene Ontology Cellular Component

Saccharomyces cerevisiae (S288c)
PREY

CDC36

DNA19, NOT2, CCR4-NOT core subunit CDC36, L000000272, YDL165W
Component of the CCR4-NOT core complex; this complex has multiple roles in regulating mRNA levels including regulation of transcription and destabilizing mRNAs through deadenylation; basal transcription factor
Saccharomyces cerevisiae (S288c)

Affinity Capture-RNA

An interaction is inferred when a bait protein is affinity captured from cell extracts by either polyclonal antibody or epitope tag and associated RNA species identified by Northern blot, RT-PCR, affinity labeling, sequencing, or microarray analysis.

Publication

The Lsm1-7/Pat1 complex binds to stress-activated mRNAs and modulates the response to hyperosmotic shock.

Garre E, Pelechano V, Sanchez Del Pino M, Alepuz P, Sunnerhagen P

RNA-binding proteins (RBPs) establish the cellular fate of a transcript, but an understanding of these processes has been limited by a lack of identified specific interactions between RNA and protein molecules. Using MS2 RNA tagging, we have purified proteins associated with individual mRNA species induced by osmotic stress, STL1 and GPD1. We found members of the Lsm1-7/Pat1 RBP complex to ... [more]

PLoS Genet. Dec. 01, 2017; 14(7);e1007563 [Pubmed: 30059503]

Throughput

  • High Throughput

Curated By

  • BioGRID