Structural highlights
Function
DDX42_HUMAN ATP-dependent RNA helicase. Binds to partially double-stranded RNAs (dsRNAs) in order to unwind RNA secondary structures. Unwinding is promoted in the presence of single-strand binding proteins. Mediates also RNA duplex formation thereby displacing the single-strand RNA binding protein. ATP and ADP modulate its activity: ATP binding and hydrolysis by DDX42 triggers RNA strand separation, whereas the ADP-bound form of the protein triggers annealing of complementary RNA strands. Involved in the survival of cells by interacting with TP53BP2 and thereby counteracting the apoptosis-stimulating activity of TP53BP2. Relocalizes TP53BP2 to the cytoplasm.[1] [2]
See Also
References
- ↑ Uhlmann-Schiffler H, Jalal C, Stahl H. Ddx42p--a human DEAD box protein with RNA chaperone activities. Nucleic Acids Res. 2006 Jan 5;34(1):10-22. PMID:16397294 doi:10.1093/nar/gkj403
- ↑ Uhlmann-Schiffler H, Kiermayer S, Stahl H. The DEAD box protein Ddx42p modulates the function of ASPP2, a stimulator of apoptosis. Oncogene. 2009 May 21;28(20):2065-73. doi: 10.1038/onc.2009.75. Epub 2009 Apr 20. PMID:19377511 doi:10.1038/onc.2009.75