DHX29

Function

This gene encodes a member of the DEAH (Asp-Glu-Ala-His) subfamily of proteins, part of the DEAD (Asp-Glu-Ala-Asp) box family of RNA helicases. The encoded protein functions in translation initiation, and is specifically required for ribosomal scanning across stable mRNA secondary structures during initiation codon selection.[6] This protein may also play a role in sensing virally derived cytosolic nucleic acids.[7] Knockdown of this gene results in reduced protein translation and impaired proliferation of cancer cells.[8]

Interactions

DHX29 has been shown to interact with the eukaryotic small ribosomal subunit (40S) and eIF3.[9][10][11][12]

See also

References

  1. GRCh38: Ensembl release 89: ENSG00000067248 - Ensembl, May 2017
  2. GRCm38: Ensembl release 89: ENSMUSG00000042426 - Ensembl, May 2017
  3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. "Entrez Gene: DExH-box helicase 29".
  6. Pisareva VP, Pisarev AV, Komar AA, Hellen CU, Pestova TV (December 2008). "Translation initiation on mammalian mRNAs with structured 5'UTRs requires DExH-box protein DHX29". Cell. 135 (7): 1237–50. doi:10.1016/j.cell.2008.10.037. PMC 2948571. PMID 19109895.
  7. Sugimoto N, Mitoma H, Kim T, Hanabuchi S, Liu YJ (May 2014). "Helicase proteins DHX29 and RIG-I cosense cytosolic nucleic acids in the human airway system". Proceedings of the National Academy of Sciences of the United States of America. 111 (21): 7747–52. doi:10.1073/pnas.1400139111. PMC 4040624. PMID 24821782.
  8. Parsyan A, Shahbazian D, Martineau Y, Petroulakis E, Alain T, Larsson O, Mathonnet G, Tettweiler G, Hellen CU, Pestova TV, Svitkin YV, Sonenberg N (December 2009). "The helicase protein DHX29 promotes translation initiation, cell proliferation, and tumorigenesis". Proceedings of the National Academy of Sciences of the United States of America. 106 (52): 22217–22. doi:10.1073/pnas.0909773106. PMC 2799747. PMID 20018725.
  9. Hashem Y, des Georges A, Dhote V, Langlois R, Liao HY, Grassucci RA, Hellen CU, Pestova TV, Frank J (May 2013). "Structure of the mammalian ribosomal 43S preinitiation complex bound to the scanning factor DHX29". Cell. 153 (5): 1108–19. doi:10.1016/j.cell.2013.04.036. PMC 3730827. PMID 23706745.
  10. Hashem Y, des Georges A, Dhote V, Langlois R, Liao HY, Grassucci RA, Pestova TV, Hellen CU, Frank J (November 2013). "Hepatitis-C-virus-like internal ribosome entry sites displace eIF3 to gain access to the 40S subunit". Nature. 503 (7477): 539–43. doi:10.1038/nature12658. PMC 4106463. PMID 24185006.
  11. Pisareva VP, Pisarev AV (December 2016). "DHX29 and eIF3 cooperate in ribosomal scanning on structured mRNAs during translation initiation". RNA. 22 (12): 1859–1870. doi:10.1261/rna.057851.116. PMC 5113206. PMID 27733651.
  12. des Georges A, Dhote V, Kuhn L, Hellen CU, Pestova TV, Frank J, Hashem Y (September 2015). "Structure of mammalian eIF3 in the context of the 43S preinitiation complex". Nature. 525 (7570): 491–5. doi:10.1038/nature14891. PMC 4719162. PMID 26344199.

Further reading

This article incorporates text from the United States National Library of Medicine, which is in the public domain.


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