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DHX29





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DExH-box helicase 29 (DHX29) is a 155 kDa protein that in humans is encoded by the DHX29 gene.[5]

DHX29
Identifiers
AliasesDHX29, DDX29, DEAH-box helicase 29, DExH-box helicase 29
External IDsOMIM: 612720; MGI: 2145374; HomoloGene: 10387; GeneCards: DHX29; OMA:DHX29 - orthologs
Orthologs
SpeciesHumanMouse
Entrez

54505

218629

Ensembl

ENSG00000067248

ENSMUSG00000042426

UniProt

Q7Z478

Q6PGC1

RefSeq (mRNA)

NM_019030
NM_001345964
NM_001345965

NM_172594

RefSeq (protein)

NP_001332893
NP_001332894
NP_061903

NP_766182

Location (UCSC)Chr 5: 55.26 – 55.31 MbChr 13: 113.06 – 113.11 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

Function

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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

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

See also

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References

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000067248 – Ensembl, May 2017
  • ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000042426 – Ensembl, May 2017
  • ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  • ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  • ^ "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. PMC 2948571. 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. Bibcode:2014PNAS..111.7747S. 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. Bibcode:2009PNAS..10622217P. 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. PMC 3730827. 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. Bibcode:2013Natur.503..539H. doi:10.1038/nature12658. PMC 4106463. 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. PMC 5113206. 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. Bibcode:2015Natur.525..491D. doi:10.1038/nature14891. PMC 4719162. PMID 26344199.

    • Further reading

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  • 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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    Last edited on 17 October 2022, at 09:41  





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