Disconnected Interacting Protein 1 binds with high affinity to pre-tRNA and ADAT.

Disconnected Interacting Protein 1 (DIP1), a member of the double-stranded RNA-binding protein family based on amino acid sequence, was shown previously to form complexes with multiple transcription factors in Drosophila melanogaster. To explore this protein further, we have undertaken sedimentation equilibrium experiments that demonstrate that DIP1-c (longest isoform of DIP1) is a dimer in solution, a characteristic common to other members of the dsRNA-binding protein family. The closest sequence identity for DIP1 is found within the dsRBD sequences of RNA editase enzymes. Consistent with this role, we demonstrate binding of DIP1-c to a potential physiological RNA target: pre-tRNA. In addition, DIP1-c was shown to interact with ADAT, a tRNA deaminase that presumably modifies pre-tRNAs. From these data, we hypothesize that DIP1 may serve an integrator role by binding its dsRNA ligand and recruiting protein partners for the appropriate metabolism of the bound RNA.

Catanese DJ Jr ，Matthews KS 《-》

Hox transcription factor ultrabithorax Ib physically and genetically interacts with disconnected interacting protein 1, a double-stranded RNA-binding protein.

Bondos SE ，Catanese DJ Jr ，Tan XX ，Bicknell A ，Li L ，Matthews KS ... -  《JOURNAL OF BIOLOGICAL CHEMISTRY》

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 DJ Jr ，Matthews KS 《-》

A novel double-stranded RNA-binding protein, disco interacting protein 1 (DIP1), contributes to cell fate decisions during Drosophila development.

DeSousa D ，Mukhopadhyay M ，Pelka P ，Zhao X ，Dey BK ，Robert V ，Pélisson A ，Bucheton A ，Campos AR ... -  《JOURNAL OF BIOLOGICAL CHEMISTRY》

The properties of a tRNA-specific adenosine deaminase from Drosophila melanogaster support an evolutionary link between pre-mRNA editing and tRNA modification.

Keegan LP ，Gerber AP ，Brindle J ，Leemans R ，Gallo A ，Keller W ，O'Connell MA ... -  《-》