BAIT
OXP1
YKL215C
5-oxoprolinase; enzyme is ATP-dependent and functions as a dimer; similar to mouse Oplah gene; green fluorescent protein (GFP)-fusion protein localizes to the cytoplasm; protein abundance increases in response to DNA replication stress
GO Process (1)
GO Function (1)
GO Component (1)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Saccharomyces cerevisiae (S288c)
PREY
PMP1
L000001453, YCR024C-A
Regulatory subunit for the plasma membrane H(+)-ATPase Pma1p; small single-membrane span proteolipid; forms unique helix and positively charged cytoplasmic domain that is able to specifically segregate phosphatidylserines; PMP1 has a paralog, PMP2, that arose from the whole genome duplication
GO Process (1)
GO Function (1)
GO Component (2)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
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 elongation factor eEF3 (Yef3) interacts with mRNA in a translation independent manner.
mRNA binding proteins (RBPs) constitute 10-15% of the eukaryotic proteome and play important part in post-transcriptional regulation of gene expression. Due to the instability of RNA and the transient nature its interaction with RBPs, identification of novel RBPs is a significant challenge. Recently, a novel methodology for RBP purification and identification (termed RaPID) was presented, which allows high affinity purification ... [more]
BMC Mol. Biol. Sep. 24, 2015; 16(0);17 [Pubmed: 26404137]
Throughput
- High Throughput
Additional Notes
- PMP1 mRNA
- RaPID procedure
Curated By
- BioGRID