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

Gene Ontology Cellular Component

Saccharomyces cerevisiae (S288c)
PREY

SNR57

L000004526
C/D box small nucleolar RNA (snoRNA); guides 2'-O-methylation of small subunit (SSU) rRNA at position G1572
GO Process (0)
GO Function (0)
GO Component (0)
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.

Porter DF, Koh YY, VanVeller B, Raines RT, Wickens M

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