DHX36

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DEAH (Asp-Glu-Ala-His) box polypeptide 36
Identifiers
Symbols DHX36 ; DDX36; G4R1; MLEL1; RHAU
External IDs OMIM612767 MGI1919412 HomoloGene6356 GeneCards: DHX36 Gene
EC number 3.6.4.12, 3.6.4.13
Orthologs
Species Human Mouse
Entrez 170506 72162
Ensembl ENSG00000174953 ENSMUSG00000027770
UniProt Q9H2U1 Q8VHK9
RefSeq (mRNA) NM_001114397 NM_028136
RefSeq (protein) NP_001107869 NP_082412
Location (UCSC) Chr 3:
153.99 – 154.04 Mb
Chr 3:
62.47 – 62.51 Mb
PubMed search [1] [2]

Probable ATP-dependent RNA helicase DHX36 also known as DEAH box protein 36 (DHX36) or MLE-like protein 1 (MLEL1) or G4 resolvase (G4R1) or RNA helicase associated with AU-rich elements (RHAU) is an enzyme that in humans is encoded by the DHX36 gene.[1][2]

Structure[edit]

Structurally, RHAU is a 1008 amino acid-long modular protein. It consists of a ~440-amino acid helicase core comprising all signature motifs of the DEAH-box family of helicases with N- and C-terminal flanking regions of ~180 and ~380 amino acids, respectively. Like all the DEAH-box proteins, the helicase associated domain is located adjacent to the helicase core region and occupies 75% of the C-terminal region.

Function[edit]

DEAD box proteins, characterized by the conserved motif Asp-Glu-Ala-Asp (DEAD), 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 DEAD box protein family are believed to be involved in embryogenesis, spermatogenesis, and cellular growth and division.[1]

RHAU exhibits a unique ATP-dependent guanine-quadruplex (G4) resolvase activity and specificity for its substrate in vitro.[3][4] RHAU binds G4-nucleic acid with sub-nanomolar affinity and unwinds G4 structures much more efficiently than double-stranded nucleic acid. Consistent with these biochemical observations, RHAU was also identified as the major source of tetramolecular RNA-resolving activity in HeLa cell lysates.

Previous work showed that RHAU associates with mRNAs and re-localises to stress granules (SGs) upon translational arrest induced by various environmental stresses.[5][6] A region of the first 105 amino acid was shown to be critical for RNA binding and re-localisation to SGs.

References[edit]

  1. ^ a b "Entrez Gene: DHX36 DEAH (Asp-Glu-Ala-His) box polypeptide 36". 
  2. ^ Abdelhaleem M, Maltais L, Wain H (June 2003). "The human DDX and DHX gene families of putative RNA helicases". Genomics 81 (6): 618–22. doi:10.1016/S0888-7543(03)00049-1. PMID 12782131. 
  3. ^ Vaughn JP, Creacy SD, Routh ED, Joyner-Butt C, Jenkins GS, Pauli S, Nagamine Y, Akman SA (November 2005). "The DEXH protein product of the DHX36 gene is the major source of tetramolecular quadruplex G4-DNA resolving activity in HeLa cell lysates". J. Biol. Chem. 280 (46): 38117–20. doi:10.1074/jbc.C500348200. PMID 16150737. 
  4. ^ Creacy SD, Routh ED, Iwamoto F, Nagamine Y, Akman SA, Vaughn JP (December 2008). "G4 Resolvase 1 Binds Both DNA and RNA Tetramolecular Quadruplex with High Affinity and Is the Major Source of Tetramolecular Quadruplex G4-DNA and G4-RNA Resolving Activity in HeLa Cell Lysates". J. Biol. Chem. 283 (50): 34626–34. doi:10.1074/jbc.M806277200. PMC 2596407. PMID 18842585. 
  5. ^ Chalupníková K, Lattmann S, Selak N, Iwamoto F, Fujiki Y, Nagamine Y (December 2008). "Recruitment of the RNA helicase RHAU to stress granules via a unique RNA-binding domain". J. Biol. Chem. 283 (50): 35186–98. doi:10.1074/jbc.M804857200. PMC 3259895. PMID 18854321. 
  6. ^ Chalupníková, Kateřina (2008). "Characterizing functional domains of the RNA helicase RHAU involved in subcellular localization and RNA interaction". [unreliable medical source?]

Further reading[edit]

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