FB2026_03 , released September 17, 2026
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Citation
Catanese, D.J., Matthews, K.S. (2010). High affinity, dsRNA binding by disconnected interacting protein 1.  Biochem. Biophys. Res. Commun. 399(2): 186--191.
FlyBase ID
FBrf0211599
Publication Type
Research paper
Abstract
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.
PubMed ID
PubMed Central ID
PMC2931317 (PMC) (EuropePMC)
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Secondary IDs
    Language of Publication
    English
    Additional Languages of Abstract
    Parent Publication
    Publication Type
    Journal
    Abbreviation
    Biochem. Biophys. Res. Commun.
    Title
    Biochemical and Biophysical Research Communications
    Publication Year
    1959-
    ISBN/ISSN
    0006-291X
    Data From Reference
    Genes (2)
    Physical Interactions (1)