BAIT
BFR1
L000000174, YOR198C
Component of mRNP complexes associated with polyribosomes; involved in localization of mRNAs to P bodies; implicated in secretion and nuclear segregation; multicopy suppressor of BFA (Brefeldin A) sensitivity
GO Process (4)
GO Function (2)
GO Component (5)
Gene Ontology Biological Process
Gene Ontology Molecular Function
Gene Ontology Cellular Component
Saccharomyces cerevisiae (S288c)
PREY
RPL40A
CEP52A, UB11, UBI1, ubiquitin-ribosomal 60S subunit protein L40A fusion protein, L40e, L40A, L000002411, L000000313, YIL148W
Ubiquitin-ribosomal 60S subunit protein L40A fusion protein; cleaved to yield ubiquitin and ribosomal protein L40A; ubiquitin may facilitate assembly of the ribosomal protein into ribosomes; homologous to mammalian ribosomal protein L40, no bacterial homolog; RPL40A has a paralog, RPL40B, that arose from the whole genome duplication; relative distribution to the nucleus increases upon DNA replication stress
GO Process (5)
GO Function (2)
GO Component (3)
Gene Ontology Biological Process
Gene Ontology Molecular Function
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
Protein-RNA networks revealed through covalent RNA marks.
Protein-RNA networks are ubiquitous and central in biological control. We present an approach termed RNA Tagging that enables the user to identify protein-RNA interactions in vivo by analyzing purified cellular RNA, without protein purification or cross-linking. An RNA-binding protein of interest is fused to an enzyme that adds uridines to the end of RNA. RNA targets bound by the chimeric ... [more]
Nat. Methods Dec. 01, 2015; 12(12);1163-70 [Pubmed: 26524240]
Throughput
- High Throughput
Additional Notes
- RNA Tagging
Curated By
- BioGRID