High affinity, dsRNA binding by disconnected interacting protein 1.
Disconnected interacting protein 1 (DIP1) appears from sequence analysis and preliminary binding studies to be a member of the dsRNA-binding protein family. Of interest, DIP1 was shown previously to interact with and influence multiple proteins involved in transcription regulation in Drosophila melanogaster. We show here that the longest isoform of this protein, DIP1-c, exhibits a 500-fold preference for dsRNA over dsDNA of similar nucleotide sequence. Further, DIP1-c demonstrated very high affinity for a subset of dsRNA ligands, with binding in the picomolar range for VA1 RNA and miR-iab-4 precursor stem-loop, a potential physiological RNA target involved in regulating expression of its protein partner, Ultrabithorax.
Catanese
Daniel J
DJ
Department of Biochemistry and Cell Biology, Rice University, 6100 Main St., Houston, TX 77005, United States. catanese@bcm.edu
Matthews
Kathleen S
KS
D001483:Base Sequence; D029721:Drosophila Proteins / Q000737:chemistry*; D024202:Electrophoretic Mobility Shift Assay; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D011485:Protein Binding; D012330:RNA, Double-Stranded / Q000737:chemistry*; D012367:RNA, Viral / Q000737:chemistry; D014157:Transcription Factors / Q000737:chemistry*
C410062:DISCO Interacting Protein 1, Drosophila; D029721:Drosophila Proteins; D012330:RNA, Double-Stranded; D012367:RNA, Viral; D014157:Transcription Factors; C052835:adenovirus associated RNA