BAIT
PUF2
YPR042C
PUF family mRNA-binding protein; Pumilio homology domain confers RNA binding activity; preferentially binds mRNAs encoding membrane-associated proteins; binding site composed of two UAAU tetranucleotides, separated by a 3-nt linker; PUF2 has a paralog, JSN1, that arose from the whole genome duplication
GO Process (1)
GO Function (1)
GO Component (1)
Gene Ontology Biological Process
Gene Ontology Molecular Function- mRNA binding [IDA, ISS]
- mRNA binding [IDA, ISS]
Saccharomyces cerevisiae (S288c)
PREY
PDR5
LEM1, STS1, YDR1, ATP-binding cassette multidrug transporter PDR5, L000001365, L000002136, L000002504, YOR153W
Plasma membrane ATP-binding cassette (ABC) transporter; multidrug transporter actively regulated by Pdr1p; also involved in steroid transport, cation resistance, and cellular detoxification during exponential growth; PDR5 has a paralog, PDR15, that arose from the whole genome duplication
GO Process (3)
GO Function (1)
GO Component (3)
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
Target selection by natural and redesigned PUF proteins.
Pumilio/fem-3 mRNA binding factor (PUF) proteins bind RNA with sequence specificity and modularity, and have become exemplary scaffolds in the reengineering of new RNA specificities. Here, we report the in vivo RNA binding sites of wild-type (WT) and reengineered forms of the PUF protein Saccharomyces cerevisiae Puf2p across the transcriptome. Puf2p defines an ancient protein family present throughout fungi, with ... [more]
Proc. Natl. Acad. Sci. U.S.A. Dec. 29, 2015; 112(52);15868-73 [Pubmed: 26668354]
Throughput
- High Throughput
Additional Notes
- HITS-CLIP
- PAR-CLIP
Curated By
- BioGRID