RNA Helicase A

ATP-dependent RNA helicase A (RHA; also known as DHX9, LKP, and NDHI) is an enzyme that in humans is encoded by the DHX9 gene.

DHX9
Available structures PDB Ortholog search: PDBe RCSB List of PDB id codes 3LLM, 3VYX, 3VYY
Identifiers
Aliases	DHX9, DDX9, LKP, NDH2, NDHII, RHA, RNA Helicase A, DEAH-box helicase 9, DExH-box helicase 9
External IDs	OMIM: 603115; MGI: 108177; HomoloGene: 1039; GeneCards: DHX9; OMA:DHX9 - orthologs
Gene location (Human) Chr. Chromosome 1 (human) Band 1q25.3 Start 182,839,347 bp End 182,887,982 bp
Gene location (Mouse) Chr. Chromosome 1 (mouse) Band 1 G3|1 65.37 cM Start 153,331,504 bp End 153,363,406 bp
RNA expression pattern Bgee Human Mouse (ortholog) Top expressed in ventricular zone ganglionic eminence sperm Achilles tendon right ovary left ovary right testis canal of the cervix body of uterus left testis Top expressed in tail of embryo primitive streak abdominal wall otic placode mandibular prominence maxillary prominence Gonadal ridge vas deferens saccule otic vesicle More reference expression data BioGPS More reference expression data
Gene ontology Molecular function RNA helicase activity nucleotide binding helicase activity protein binding nucleic acid binding hydrolase activity RNA binding DNA binding single-stranded DNA binding double-stranded RNA binding single-stranded RNA binding nucleoside-triphosphatase activity chromatin DNA binding 3'-5' DNA/RNA helicase activity 3'-5' RNA helicase activity triplex DNA binding nucleoside-triphosphate diphosphatase activity importin-alpha family protein binding single-stranded 3'-5' DNA helicase activity siRNA binding mRNA binding RNA stem-loop binding polysome binding promoter-specific chromatin binding RNA polymerase II complex binding regulatory region RNA binding transcription coregulator activity transcription coactivator activity DNA replication origin binding double-stranded DNA binding DNA helicase activity ATP binding ATPase activity RNA polymerase binding 3'-5' DNA helicase activity RISC complex binding sequence-specific mRNA binding metal ion binding RNA polymerase II cis-regulatory region sequence-specific DNA binding Cellular component CRD-mediated mRNA stability complex cytosol centrosome membrane cytoplasmic ribonucleoprotein granule nucleus nucleolus perichromatin fibrils cytoplasm nuclear stress granule nuclear body polysomal ribosome polysome actin cytoskeleton RISC-loading complex nucleoplasm microtubule organizing center cytoskeleton protein-containing complex ribonucleoprotein complex Biological process CRD-mediated mRNA stabilization mRNA splicing, via spliceosome RNA processing rhythmic process protein localization to cytoplasmic stress granule osteoblast differentiation positive regulation of type I interferon production RNA secondary structure unwinding positive regulation of DNA repair positive regulation of transcription by RNA polymerase II positive regulation of response to cytokine stimulus cellular response to exogenous dsRNA alternative mRNA splicing, via spliceosome DNA-templated viral transcription positive regulation of viral transcription positive regulation of viral translation positive regulation of cytoplasmic translation regulation of transcription by RNA polymerase II DNA duplex unwinding positive regulation of DNA replication positive regulation of fibroblast proliferation regulation of mRNA processing positive regulation of NF-kappaB transcription factor activity cellular response to tumor necrosis factor positive regulation of DNA topoisomerase (ATP-hydrolyzing) activity regulation of cytoplasmic translation positive regulation of interleukin-18 production G-quadruplex DNA unwinding positive regulation of innate immune response positive regulation of RNA export from nucleus regulation of defense response to virus by host positive regulation of inflammatory response pyroptosis small RNA loading onto RISC positive regulation of polysome binding positive regulation of gene silencing by miRNA immune system process DNA replication transcription, DNA-templated DNA-templated transcription, termination regulation of transcription, DNA-templated mRNA processing regulation of translation transport inflammatory response RNA splicing gene silencing innate immune response mRNA transport Sources:Amigo / QuickGO
Orthologs Species Human Mouse Entrez 1660 13211 Ensembl ENSG00000135829 ENSMUSG00000042699 UniProt Q08211 O70133 RefSeq (mRNA) NM_001357 NM_030588 NM_007842 RefSeq (protein) NP_001348 NP_031868 NP_001392438 Location (UCSC) Chr 1: 182.84 – 182.89 Mb Chr 1: 153.33 – 153.36 Mb PubMed search
Wikidata
View/Edit Human View/Edit Mouse

Function

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. The DHX9 gene is located on the long arm q of chromosome 1.

Interactions

DHX9 has been shown to interact with:

• AKAP8L,
• BRCA1,
• DDX17 (p72)
• DDX5 (p68),
• KHDRBS1,
• MIZF,
• NXF1,
• PRMT1,
• RELA, and
• SMN1.

Further reading

• 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. doi:10.1016/S0021-9258(18)42849-9. PMID 1537828.
• 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. doi:10.1016/S0021-9258(19)38673-9. PMID 7685763.
• 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. doi:10.4049/jimmunol.156.6.2026. PMID 8690889. S2CID 24465550.
• 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. PMID 9323138. S2CID 16819946.
• Loor G, Zhang SJ, Zhang P, Toomey NL, Lee MY (Dec 1997). "Identification of DNA replication and cell cycle proteins that interact with PCNA". Nucleic Acids Research. 25 (24): 5041–6. doi:10.1093/nar/25.24.5041. PMC 147130. PMID 9396813.
• 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. PMID 9480750.
• 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. PMID 9662397. S2CID 10953768.
• Lee CG, da Costa Soares V, Newberger C, Manova K, Lacy E, Hurwitz J (Nov 1998). "RNA helicase A is essential for normal gastrulation". Proceedings of the National Academy of Sciences of the United States of America. 95 (23): 13709–13. Bibcode:1998PNAS...9513709L. doi:10.1073/pnas.95.23.13709. PMC 24884. PMID 9811865.
• Li J, Tang H, Mullen TM, Westberg C, Reddy TR, Rose DW, Wong-Staal F (Jan 1999). "A role for RNA helicase A in post-transcriptional regulation of HIV type 1". Proceedings of the National Academy of Sciences of the United States of America. 96 (2): 709–14. Bibcode:1999PNAS...96..709L. doi:10.1073/pnas.96.2.709. PMC 15201. PMID 9892698.
• Tang H, McDonald D, Middlesworth T, Hope TJ, Wong-Staal F (May 1999). "The carboxyl terminus of RNA helicase A contains a bidirectional nuclear transport domain". Molecular and Cellular Biology. 19 (5): 3540–50. doi:10.1128/mcb.19.5.3540. PMC 84146. PMID 10207077.
• 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. PMID 10748171.
• 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. PMID 10924507.
• 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. PMID 10925702. S2CID 29684315.
• 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. PMID 10951562.
• Pellizzoni L, Charroux B, Rappsilber J, Mann M, Dreyfuss G (Jan 2001). "A functional interaction between the survival motor neuron complex and RNA polymerase II". The Journal of Cell Biology. 152 (1): 75–85. doi:10.1083/jcb.152.1.75. PMC 2193649. PMID 11149922.
• 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. PMID 11254741.
• 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. PMID 11402034.
• Aratani S, Fujii R, Oishi T, Fujita H, Amano T, Ohshima T, Hagiwara M, Fukamizu A, Nakajima T (Jul 2001). "Dual roles of RNA helicase A in CREB-dependent transcription". Molecular and Cellular Biology. 21 (14): 4460–9. doi:10.1128/MCB.21.14.4460-4469.2001. PMC 87106. PMID 11416126.