| Structural highlights
Function
DDX1_HUMAN Acts as an ATP-dependent RNA helicase, able to unwind both RNA-RNA and RNA-DNA duplexes. Possesses 5' single-stranded RNA overhang nuclease activity. Possesses ATPase activity on various RNA, but not DNA polynucleotides. May play a role in RNA clearance at DNA double-strand breaks (DSBs), thereby facilitating the template-guided repair of transcriptionally active regions of the genome. Together with RELA, acts as a coactivator to enhance NF-kappa-B-mediated transcriptional activation. Acts as a positive transcriptional regulator of cyclin CCND2 expression. Binds to the cyclin CCND2 promoter region. Associates with chromatin at the NF-kappa-B promoter region via association with RELA. Binds to poly(A) RNA. May be involved in 3'-end cleavage and polyadenylation of pre-mRNAs. Component of the tRNA-splicing ligase complex required to facilitate the enzymatic turnover of catalytic subunit RTCB: together with archease (ZBTB8OS), acts by facilitating the guanylylation of RTCB, a key intermediate step in tRNA ligation (PubMed:24870230). Component of a multi-helicase-TICAM1 complex that acts as a cytoplasmic sensor of viral double-stranded RNA (dsRNA) and plays a role in the activation of a cascade of antiviral responses including the induction of pro-inflammatory cytokines via the adapter molecule TICAM1. Specifically binds (via helicase ATP-binding domain) on both short and long poly(I:C) dsRNA (By similarity).[UniProtKB:Q91VR5][1] [2] [3] [4] [5] [6] (Microbial infection) Required for HIV-1 Rev function as well as for HIV-1 and coronavirus IBV replication. Binds to the RRE sequence of HIV-1 mRNAs.[7] (Microbial infection) Required for Coronavirus IBV replication.[8]
References
- ↑ Chen HC, Lin WC, Tsay YG, Lee SC, Chang CJ. An RNA helicase, DDX1, interacting with poly(A) RNA and heterogeneous nuclear ribonucleoprotein K. J Biol Chem. 2002 Oct 25;277(43):40403-9. PMID:12183465 doi:10.1074/jbc.M206981200
- ↑ Fang J, Kubota S, Yang B, Zhou N, Zhang H, Godbout R, Pomerantz RJ. A DEAD box protein facilitates HIV-1 replication as a cellular co-factor of Rev. Virology. 2004 Dec 20;330(2):471-80. PMID:15567440 doi:10.1016/j.virol.2004.09.039
- ↑ Onishi H, Kino Y, Morita T, Futai E, Sasagawa N, Ishiura S. MBNL1 associates with YB-1 in cytoplasmic stress granules. J Neurosci Res. 2008 Jul;86(9):1994-2002. doi: 10.1002/jnr.21655. PMID:18335541 doi:10.1002/jnr.21655
- ↑ Li L, Monckton EA, Godbout R. A role for DEAD box 1 at DNA double-strand breaks. Mol Cell Biol. 2008 Oct;28(20):6413-25. PMID:18710941 doi:10.1128/MCB.01053-08
- ↑ Xu L, Khadijah S, Fang S, Wang L, Tay FP, Liu DX. The cellular RNA helicase DDX1 interacts with coronavirus nonstructural protein 14 and enhances viral replication. J Virol. 2010 Sep;84(17):8571-83. PMID:20573827 doi:10.1128/JVI.00392-10
- ↑ Popow J, Jurkin J, Schleiffer A, Martinez J. Analysis of orthologous groups reveals archease and DDX1 as tRNA splicing factors. Nature. 2014 Jul 3;511(7507):104-7. PMID:24870230 doi:10.1038/nature13284
- ↑ Fang J, Kubota S, Yang B, Zhou N, Zhang H, Godbout R, Pomerantz RJ. A DEAD box protein facilitates HIV-1 replication as a cellular co-factor of Rev. Virology. 2004 Dec 20;330(2):471-80. PMID:15567440 doi:10.1016/j.virol.2004.09.039
- ↑ Xu L, Khadijah S, Fang S, Wang L, Tay FP, Liu DX. The cellular RNA helicase DDX1 interacts with coronavirus nonstructural protein 14 and enhances viral replication. J Virol. 2010 Sep;84(17):8571-83. PMID:20573827 doi:10.1128/JVI.00392-10
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