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    DHX36 DEAH-box helicase 36 [ Homo sapiens (human) ]

    Gene ID: 170506, updated on 5-May-2024

    GeneRIFs: Gene References Into Functions

    GeneRIFPubMed TitleDate
    Differential Gene Expression following DHX36/G4R1 Knockout Is Associated with G-Quadruplex Content and Cancer.

    Differential Gene Expression following DHX36/G4R1 Knockout Is Associated with G-Quadruplex Content and Cancer.
    Gumina JM, Richardson AE, Shojiv MH, Chambers AE, Sandwith SN, Reisinger MA, Karns TJ, Osborne TL, Alashi HN, Anderson QT, Sharlow ME, Seiler DC, Rogers EM, Bartosik AR, Smaldino MA, Vaughn JP, Wang YH, Smaldino PJ, Haney RA., Free PMC Article

    02/28/2024
    G-Quadruplexes and the DNA/RNA helicase DHX36 in health, disease, and aging.

    G-Quadruplexes and the DNA/RNA helicase DHX36 in health, disease, and aging.
    Antcliff A, McCullough LD, Tsvetkov AS., Free PMC Article

    02/19/2022
    G4-PROTAC: targeted degradation of a G-quadruplex binding protein.

    G4-PROTAC: targeted degradation of a G-quadruplex binding protein.
    Patil KM, Chin D, Seah HL, Shi Q, Lim KW, Phan AT.

    12/18/2021
    The RNA helicase DHX36-G4R1 modulates C9orf72 GGGGCC hexanucleotide repeat-associated translation.

    The RNA helicase DHX36-G4R1 modulates C9orf72 GGGGCC hexanucleotide repeat-associated translation.
    Tseng YJ, Sandwith SN, Green KM, Chambers AE, Krans A, Raimer HM, Sharlow ME, Reisinger MA, Richardson AE, Routh ED, Smaldino MA, Wang YH, Vaughn JP, Todd PK, Smaldino PJ., Free PMC Article

    12/4/2021
    The DEAH helicase DHX36 and its role in G-quadruplex-dependent processes.

    The DEAH helicase DHX36 and its role in G-quadruplex-dependent processes.
    Schult P, Paeschke K.

    11/6/2021
    The DHX36-specific-motif (DSM) enhances specificity by accelerating recruitment of DNA G-quadruplex structures.

    The DHX36-specific-motif (DSM) enhances specificity by accelerating recruitment of DNA G-quadruplex structures.
    Chang-Gu B, Bradburn D, Yangyuoru PM, Russell R., Free PMC Article

    11/6/2021
    DHX36, BAX, and ARPC1B May Be Critical for the Diagnosis and Treatment of Tuberculosis.

    DHX36, BAX, and ARPC1B May Be Critical for the Diagnosis and Treatment of Tuberculosis.
    Zhang Y, Li Y, Li H, Liu Q, Wang W, Jian Z, Liu W., Free PMC Article

    09/11/2021
    Recognition of different base tetrads by RHAU (DHX36): X-ray crystal structure of the G4 recognition motif bound to the 3'-end tetrad of a DNA G-quadruplex.

    Recognition of different base tetrads by RHAU (DHX36): X-ray crystal structure of the G4 recognition motif bound to the 3'-end tetrad of a DNA G-quadruplex.
    Heddi B, Cheong VV, Schmitt E, Mechulam Y, Phan AT.

    04/17/2021
    Considering that DHX36 targets, harboring G4s, preferentially localize in stress granules, and that DHX36 KO results in increased SG formation and protein kinase R (PKR/EIF2AK2) phosphorylation, we speculate that DHX36 is involved in resolution of rG4 induced cellular stress.

    DHX36 prevents the accumulation of translationally inactive mRNAs with G4-structures in untranslated regions.
    Sauer M, Juranek SA, Marks J, De Magis A, Kazemier HG, Hilbig D, Benhalevy D, Wang X, Hafner M, Paeschke K., Free PMC Article

    06/29/2019
    Study demonstrated that unlike on G4-DNA, DHX36 displays ATP-independent unfolding of G4-RNA followed by ATP-dependent refolding, generating a highly asymmetric pattern of activity. DHX36 refolds G4-RNA in several steps, reflecting the discrete steps in forming the G4 structure. The ATP-dependent activity of DHX36 arises from the RNA tail rather than the G4.

    RNA G-quadruplex is resolved by repetitive and ATP-dependent mechanism of DHX36.
    Tippana R, Chen MC, Demeshkina NA, Ferré-D'Amaré AR, Myong S., Free PMC Article

    06/15/2019
    RNA G-quadruplex folding, controlled by the two DEAH-box helicases DHX36 and DHX9, impedes the scanning of the 43S preinitiation complex, promotes 80S ribosome formation within 5'-UTRs and consequently represses the translation of transcripts involved in key biological pathways.

    RNA G-quadruplexes at upstream open reading frames cause DHX36- and DHX9-dependent translation of human mRNAs.
    Murat P, Marsico G, Herdy B, Ghanbarian AT, Portella G, Balasubramanian S., Free PMC Article

    03/9/2019
    DHX36 has striking 3'-extension sequence preferences that differ for G4 disruption and dsDNA unwinding, most likely arising from differences in the rate-limiting step for the two activities.

    The G-quadruplex (G4) resolvase DHX36 efficiently and specifically disrupts DNA G4s via a translocation-based helicase mechanism.
    Yangyuoru PM, Bradburn DA, Liu Z, Xiao TS, Russell R., Free PMC Article

    02/16/2019
    biophysical analysis provides evidence that the RNA G-quadruplex, but not its DNA counterpart, can adopt a parallel orientation, and that only the RNA can interact with N-terminal domain of RHAU via the tetrad face of the G-quadruplex. This work extends our insight into how the N-terminal region of RHAU recognizes parallel G-quadruplexes.

    Biophysical Characterization of G-Quadruplex Recognition in the PITX1 mRNA by the Specificity Domain of the Helicase RHAU.
    Ariyo EO, Booy EP, Patel TR, Dzananovic E, McRae EK, Meier M, McEleney K, Stetefeld J, McKenna SA., Free PMC Article

    02/2/2019
    Data show that helicases RHAU, BLM, and WRN exhibit distinct G-quadruplex (GQ) conformation specificity, but use a common mechanism of repetitive unfolding that leads to disrupting GQ structure multiple times in succession.

    Single-molecule imaging reveals a common mechanism shared by G-quadruplex-resolving helicases.
    Tippana R, Hwang H, Opresko PL, Bohr VA, Myong S., Free PMC Article

    02/10/2018
    RHAU mediates the unfolding of DNA and RNA quadruplexes.

    G-quadruplexes unfolding by RHAU helicase.
    Gueddouda NM, Mendoza O, Gomez D, Bourdoncle A, Mergny JL.

    10/21/2017
    The study provides the first evidence that the unfolding kinetics of a G-quadruplex can be modulated by different nucleotide-bound states of the RHAU helicase.

    RHAU helicase stabilizes G4 in its nucleotide-free state and destabilizes G4 upon ATP hydrolysis.
    You H, Lattmann S, Rhodes D, Yan J., Free PMC Article

    06/10/2017
    RHAU binds to an adenosine-rich region near the 3'-end of the long non-coding RNA BC200.

    RNA Helicase Associated with AU-rich Element (RHAU/DHX36) Interacts with the 3'-Tail of the Long Non-coding RNA BC200 (BCYRN1).
    Booy EP, McRae EK, Howard R, Deo SR, Ariyo EO, Dzananovic E, Meier M, Stetefeld J, McKenna SA., Free PMC Article

    08/13/2016
    present a model showing that a replication fork disrupting a T-loop could create a 5' quadruplex with an opened 3'tail structure that is recognized by G4R1

    Mutational Dissection of Telomeric DNA Binding Requirements of G4 Resolvase 1 Shows that G4-Structure and Certain 3'-Tail Sequences Are Sufficient for Tight and Complete Binding.
    Smaldino PJ, Routh ED, Kim JH, Giri B, Creacy SD, Hantgan RR, Akman SA, Vaughn JP., Free PMC Article

    05/7/2016
    we identify a novel function of DHX36 to facilitate viral RNA recognition

    DHX36 enhances RIG-I signaling by facilitating PKR-mediated antiviral stress granule formation.
    Yoo JS, Takahasi K, Ng CS, Ouda R, Onomoto K, Yoneyama M, Lai JC, Lattmann S, Nagamine Y, Matsui T, Iwabuchi K, Kato H, Fujita T., Free PMC Article

    11/8/2014
    Used an integrated approach that includes small angle x-ray scattering, nuclear magnetic resonance spectroscopy, circular dichroism, and dynamic light scattering methods to demonstrate the recognition of G-quadruplexes by the N-terminal domain of RHAU.

    Binding of G-quadruplexes to the N-terminal recognition domain of the RNA helicase associated with AU-rich element (RHAU).
    Meier M, Patel TR, Booy EP, Marushchak O, Okun N, Deo S, Howard R, McEleney K, Harding SE, Stetefeld J, McKenna SA., Free PMC Article

    02/15/2014
    Data supports a helicase function of RHAU on an intramolecular RNA quadruplex and show that the enzyme is capable of completely converting quadruplex RNA to a stable duplex.

    The RNA helicase RHAU (DHX36) unwinds a G4-quadruplex in human telomerase RNA and promotes the formation of the P1 helix template boundary.
    Booy EP, Meier M, Okun N, Novakowski SK, Xiong S, Stetefeld J, McKenna SA., Free PMC Article

    07/21/2012
    Data show that hnRNPA1/A2, HuR and DAZAP1 splicing factors and DHX36 RNA helicase bind to the ISE, with hnRNPA1 acting negatively and DAZAP1 positively on splicing selection

    Interaction of hnRNPA1/A2 and DAZAP1 with an Alu-derived intronic splicing enhancer regulates ATM aberrant splicing.
    Pastor T, Pagani F., Free PMC Article

    02/18/2012
    The helicase domain of DHX36 does not mediate telomerase RNA (hTR) binding; instead, hTR interacts with the N-terminal accessory domain of DHX36 known to bind specifically to the parallel-strand G-quadruplex substrates resolved by the helicase domain.

    The 5' guanosine tracts of human telomerase RNA are recognized by the G-quadruplex binding domain of the RNA helicase DHX36 and function to increase RNA accumulation.
    Sexton AN, Collins K., Free PMC Article

    03/5/2011
    The amino-terminal region of RHAU is essential for RHAU to bind G4 structures and within this region the evolutionary conserved RSM (RHAU-specific motif) domain is a major affinity and specificity determinant

    Role of the amino terminal RHAU-specific motif in the recognition and resolution of guanine quadruplex-RNA by the DEAH-box RNA helicase RHAU.
    Lattmann S, Giri B, Vaughn JP, Akman SA, Nagamine Y., Free PMC Article

    11/6/2010
    DHX9/DHX36 represent the MyD88-dependent DNA sensors in the cytosol of plasmacytoid dendritic cells and suggest a much broader role for DHX helicases in viral sensing

    Aspartate-glutamate-alanine-histidine box motif (DEAH)/RNA helicase A helicases sense microbial DNA in human plasmacytoid dendritic cells.
    Kim T, Pazhoor S, Bao M, Zhang Z, Hanabuchi S, Facchinetti V, Bover L, Plumas J, Chaperot L, Qin J, Liu YJ., Free PMC Article

    09/27/2010
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