DHX29
DExH-box helicase 29 (DHX29) is a 155 kDa protein that in humans is encoded by the DHX29 gene.[1]
Function
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.[2] This protein may also play a role in sensing virally derived cytosolic nucleic acids.[3] Knockdown of this gene results in reduced protein translation and impaired proliferation of cancer cells.[4]
Interactions
Interactions
DHX29 has been shown to interact with the eukaryotic small ribosomal subunit (40S) and eIF3.[5][6][7][8]
References
References
- ↑ “Entrez Gene: DExH-box helicase 29”.
- ↑ 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. PMID 19109895.
- ↑ 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.
- ↑ 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.
- ↑ 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. PMID 23706745.
- ↑ 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. PMID 24185006.
- ↑ 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. PMID 27733651.
- ↑ 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. PMID 26344199.
Further reading
Further reading
- Hendrickson SL, Lautenberger JA, Chinn LW, Malasky M, Sezgin E, Kingsley LA, Goedert JJ, Kirk GD, Gomperts ED, Buchbinder SP, Troyer JL, O’Brien SJ (September 2010). “Genetic variants in nuclear-encoded mitochondrial genes influence AIDS progression”. PLOS One. 5 (9): e12862. doi:10.1371/journal.pone.0012862. PMC 2943476. PMID 20877624.
- Dhote V, Sweeney TR, Kim N, Hellen CU, Pestova TV (November 2012). “Roles of individual domains in the function of DHX29, an essential factor required for translation of structured mammalian mRNAs”. Proceedings of the National Academy of Sciences of the United States of America. 109 (46): E3150–9. doi:10.1073/pnas.1208014109. PMC 3503174. PMID 23047696.
- Pisareva VP, Pisarev AV (May 2016). “DHX29 reduces leaky scanning through an upstream AUG codon regardless of its nucleotide context”. Nucleic Acids Research. 44 (9): 4252–65. doi:10.1093/nar/gkw240. PMC 4872109. PMID 27067542.
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
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