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RHAU mediates the unfolding of DNA and RNA quadruplexes.
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 binds to an adenosine-rich region near the 3'-end of the long non-coding RNA BC200.
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
we identify a novel function of DHX36 to facilitate viral RNA recognition
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.
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.
Data show that hnRNPA1 (show HNRNPA1 Proteins)/A2, HuR (show ELAVL1 Proteins) and DAZAP1 (show DAZAP1 Proteins) splicing factors and DHX36 RNA helicase bind to the ISE, with hnRNPA1 (show HNRNPA1 Proteins) acting negatively and DAZAP1 (show DAZAP1 Proteins) positively on splicing selection
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 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
The ablation of RHAU in germ cells caused the increase of G4 structures and thus resulted in the decrease of spermatogonial differentiation.
RHAU deletion in hematopoietic system caused hemolytic anemia and differentiation defect at the proerythroblast stage. RHAU may play a role in the regulation of gene expression that relies on its G4 resolvase activity.
DDX1 (show DDX1 Proteins)-DDX21 (show DDX21 Proteins)-DHX36 complex represents a dsRNA sensor that uses the TRIF (show RNF138 Proteins) pathway to activate type I IFN responses in the cytosol of myeloid dendritic cells
This gene is a member of the DEAH-box family of RNA-dependent NTPases which are named after the conserved amino acid sequence Asp-Glu-Ala-His in motif II. The protein encoded by this gene has been shown to enhance the deadenylation and decay of mRNAs with 3'-UTR AU-rich elements (ARE-mRNA). The protein has also been shown to resolve into single strands the highly stable tetramolecular DNA configuration (G4) that can form spontaneously in guanine-rich regions of DNA. Alternative splicing results in multiple transcript variants encoding different isoforms.
probable ATP-dependent RNA helicase DHX36
, DEAH (Asp-Glu-Ala-His) box polypeptide 36
, probable ATP-dependent RNA helicase DHX36-like
, DEAD/H (Asp-Glu-Ala-Asp/His) box polypeptide 36
, DEAH box protein 36
, G4 resolvase-1
, MLE-like protein 1
, RNA helicase associated with AU-rich element ARE