DEAD/DEAH box helicases are proteins, and are putative RNA helicases. They are implicated in a number of cellular processes involving alteration of RNA secondary structure such as translation initiation, nuclear and mitochondrial splicing, and ribosome and spliceosome assembly. Based on their distribution patterns, some members of this family are believed to be involved in embryogenesis, spermatogenesis, and cellular growth and division. This gene encodes a DEAD box protein with RNA helicase activity. It may participate in melting of DNA:RNA hybrids, such as those that occur during transcription, and may play a role in X-linked gene expression. It contains 2 copies of a double-stranded RNA-binding domain, a DEXH core domain and an RGG box. The RNA-binding domains and RGG box influence and regulate RNA helicase activity.[3]The DHX9 gene is located on the long arm q of chromosome 1.
↑Lee CG, Hurwitz J (Aug 1993). "Human RNA helicase A is homologous to the maleless protein of Drosophila". The Journal of Biological Chemistry. 268 (22): 16822–30. PMID8344961.
↑Zhang S, Grosse F (Apr 1997). "Domain structure of human nuclear DNA helicase II (RNA helicase A)". The Journal of Biological Chemistry. 272 (17): 11487–94. doi:10.1074/jbc.272.17.11487. PMID9111062.
↑Yang JP, Tang H, Reddy TR, Wong-Staal F (Aug 2001). "Mapping the functional domains of HAP95, a protein that binds RNA helicase A and activates the constitutive transport element of type D retroviruses". The Journal of Biological Chemistry. 276 (33): 30694–700. doi:10.1074/jbc.M102809200. PMID11402034.
↑Westberg C, Yang JP, Tang H, Reddy TR, Wong-Staal F (Jul 2000). "A novel shuttle protein binds to RNA helicase A and activates the retroviral constitutive transport element". The Journal of Biological Chemistry. 275 (28): 21396–401. doi:10.1074/jbc.M909887199. PMID10748171.
↑Schlegel BP, Starita LM, Parvin JD (Feb 2003). "Overexpression of a protein fragment of RNA helicase A causes inhibition of endogenous BRCA1 function and defects in ploidy and cytokinesis in mammary epithelial cells". Oncogene. 22 (7): 983–91. doi:10.1038/sj.onc.1206195. PMID12592385.
↑Anderson SF, Schlegel BP, Nakajima T, Wolpin ES, Parvin JD (Jul 1998). "BRCA1 protein is linked to the RNA polymerase II holoenzyme complex via RNA helicase A". Nature Genetics. 19 (3): 254–6. doi:10.1038/930. PMID9662397.
↑Reddy TR, Tang H, Xu W, Wong-Staal F (Jul 2000). "Sam68, RNA helicase A and Tap cooperate in the post-transcriptional regulation of human immunodeficiency virus and type D retroviral mRNA". Oncogene. 19 (32): 3570–5. doi:10.1038/sj.onc.1203676. PMID10951562.
↑Tang H, Wong-Staal F (Oct 2000). "Specific interaction between RNA helicase A and Tap, two cellular proteins that bind to the constitutive transport element of type D retrovirus". The Journal of Biological Chemistry. 275 (42): 32694–700. doi:10.1074/jbc.M003933200. PMID10924507.
↑Smith WA, Schurter BT, Wong-Staal F, David M (May 2004). "Arginine methylation of RNA helicase a determines its subcellular localization". The Journal of Biological Chemistry. 279 (22): 22795–8. doi:10.1074/jbc.C300512200. PMID15084609.
↑Tetsuka T, Uranishi H, Sanda T, Asamitsu K, Yang JP, Wong-Staal F, Okamoto T (Sep 2004). "RNA helicase A interacts with nuclear factor kappaB p65 and functions as a transcriptional coactivator". European Journal of Biochemistry / FEBS. 271 (18): 3741–51. doi:10.1111/j.1432-1033.2004.04314.x. PMID15355351.
Lee CG, Hurwitz J (Mar 1992). "A new RNA helicase isolated from HeLa cells that catalytically translocates in the 3' to 5' direction". The Journal of Biological Chemistry. 267 (7): 4398–407. PMID1537828.
Lee CG, Zamore PD, Green MR, Hurwitz J (Jun 1993). "RNA annealing activity is intrinsically associated with U2AF". The Journal of Biological Chemistry. 268 (18): 13472–8. PMID7685763.
Abdelhaleem MM, Hameed S, Klassen D, Greenberg AH (Mar 1996). "Leukophysin: an RNA helicase A-related molecule identified in cytotoxic T cell granules and vesicles". Journal of Immunology. 156 (6): 2026–35. PMID8690889.
Nakajima T, Uchida C, Anderson SF, Lee CG, Hurwitz J, Parvin JD, Montminy M (Sep 1997). "RNA helicase A mediates association of CBP with RNA polymerase II". Cell. 90 (6): 1107–12. doi:10.1016/S0092-8674(00)80376-1. PMID9323138.
Lee CG, Eki T, Okumura K, da Costa Soares V, Hurwitz J (Feb 1998). "Molecular analysis of the cDNA and genomic DNA encoding mouse RNA helicase A". Genomics. 47 (3): 365–71. doi:10.1006/geno.1997.5139. PMID9480750.
Anderson SF, Schlegel BP, Nakajima T, Wolpin ES, Parvin JD (Jul 1998). "BRCA1 protein is linked to the RNA polymerase II holoenzyme complex via RNA helicase A". Nature Genetics. 19 (3): 254–6. doi:10.1038/930. PMID9662397.
Westberg C, Yang JP, Tang H, Reddy TR, Wong-Staal F (Jul 2000). "A novel shuttle protein binds to RNA helicase A and activates the retroviral constitutive transport element". The Journal of Biological Chemistry. 275 (28): 21396–401. doi:10.1074/jbc.M909887199. PMID10748171.
Tang H, Wong-Staal F (Oct 2000). "Specific interaction between RNA helicase A and Tap, two cellular proteins that bind to the constitutive transport element of type D retrovirus". The Journal of Biological Chemistry. 275 (42): 32694–700. doi:10.1074/jbc.M003933200. PMID10924507.
Lee CG, Eki T, Okumura K, Nogami M, Soares Vda C, Murakami Y, Hanaoka F, Hurwitz J (Jan 1999). "The human RNA helicase A (DDX9) gene maps to the prostate cancer susceptibility locus at chromosome band 1q25 and its pseudogene (DDX9P) to 13q22, respectively". Somatic Cell and Molecular Genetics. 25 (1): 33–9. doi:10.1023/B:SCAM.0000007138.44216.3a. PMID10925702.
Reddy TR, Tang H, Xu W, Wong-Staal F (Jul 2000). "Sam68, RNA helicase A and Tap cooperate in the post-transcriptional regulation of human immunodeficiency virus and type D retroviral mRNA". Oncogene. 19 (32): 3570–5. doi:10.1038/sj.onc.1203676. PMID10951562.
Takasaki Y, Kogure T, Takeuchi K, Kaneda K, Yano T, Hirokawa K, Hirose S, Shirai T, Hashimoto H (Apr 2001). "Reactivity of anti-proliferating cell nuclear antigen (PCNA) murine monoclonal antibodies and human autoantibodies to the PCNA multiprotein complexes involved in cell proliferation". Journal of Immunology. 166 (7): 4780–7. doi:10.4049/jimmunol.166.7.4780. PMID11254741.
Yang JP, Tang H, Reddy TR, Wong-Staal F (Aug 2001). "Mapping the functional domains of HAP95, a protein that binds RNA helicase A and activates the constitutive transport element of type D retroviruses". The Journal of Biological Chemistry. 276 (33): 30694–700. doi:10.1074/jbc.M102809200. PMID11402034.