The DEAD-box protein family of RNA helicases - PubMed (original) (raw)
Review
The DEAD-box protein family of RNA helicases
Olivier Cordin et al. Gene. 2006.
Abstract
RNA helicases of the DEAD-box protein family have been shown to participate in every aspect of RNA metabolism. They are present in most organisms where they work as RNA helicases or RNPases. The properties of these enzymes in vivo remains poorly described, however some were extensively characterized in vitro, and the solved crystal structures of a few are now available. Taken together, this information gives insight into the regulation of ATP and RNA binding as well as in the ATPase and helicase activities. This review will focus on the description of the molecular characteristics of members of the DEAD-box protein family and on the enzymatic activities they possess.
Similar articles
- Crystal structure of the human ATP-dependent splicing and export factor UAP56.
Shi H, Cordin O, Minder CM, Linder P, Xu RM. Shi H, et al. Proc Natl Acad Sci U S A. 2004 Dec 21;101(51):17628-33. doi: 10.1073/pnas.0408172101. Epub 2004 Dec 7. Proc Natl Acad Sci U S A. 2004. PMID: 15585580 Free PMC article. - DExD/H box RNA helicases: from generic motors to specific dissociation functions.
Tanner NK, Linder P. Tanner NK, et al. Mol Cell. 2001 Aug;8(2):251-62. doi: 10.1016/s1097-2765(01)00329-x. Mol Cell. 2001. PMID: 11545728 Review. - Regulation of alternative splicing by the ATP-dependent DEAD-box RNA helicase p72.
Hönig A, Auboeuf D, Parker MM, O'Malley BW, Berget SM. Hönig A, et al. Mol Cell Biol. 2002 Aug;22(16):5698-707. doi: 10.1128/MCB.22.16.5698-5707.2002. Mol Cell Biol. 2002. PMID: 12138182 Free PMC article. - The crystal structure of human DEAH-box RNA helicase 15 reveals a domain organization of the mammalian DEAH/RHA family.
Murakami K, Nakano K, Shimizu T, Ohto U. Murakami K, et al. Acta Crystallogr F Struct Biol Commun. 2017 Jun 1;73(Pt 6):347-355. doi: 10.1107/S2053230X17007336. Epub 2017 May 25. Acta Crystallogr F Struct Biol Commun. 2017. PMID: 28580923 Free PMC article. - Structure, function and regulation of spliceosomal RNA helicases.
Cordin O, Hahn D, Beggs JD. Cordin O, et al. Curr Opin Cell Biol. 2012 Jun;24(3):431-8. doi: 10.1016/j.ceb.2012.03.004. Epub 2012 Mar 29. Curr Opin Cell Biol. 2012. PMID: 22464735 Review.
Cited by
- Steady-state NTPase activity of Dengue virus NS3: number of catalytic sites, nucleotide specificity and activation by ssRNA.
Incicco JJ, Gebhard LG, González-Lebrero RM, Gamarnik AV, Kaufman SB. Incicco JJ, et al. PLoS One. 2013;8(3):e58508. doi: 10.1371/journal.pone.0058508. Epub 2013 Mar 19. PLoS One. 2013. PMID: 23526990 Free PMC article. - The DEAD-box helicase DDX3 substitutes for the cap-binding protein eIF4E to promote compartmentalized translation initiation of the HIV-1 genomic RNA.
Soto-Rifo R, Rubilar PS, Ohlmann T. Soto-Rifo R, et al. Nucleic Acids Res. 2013 Jul;41(12):6286-99. doi: 10.1093/nar/gkt306. Epub 2013 Apr 28. Nucleic Acids Res. 2013. PMID: 23630313 Free PMC article. - Human DDX3 interacts with the HIV-1 Tat protein to facilitate viral mRNA translation.
Lai MC, Wang SW, Cheng L, Tarn WY, Tsai SJ, Sun HS. Lai MC, et al. PLoS One. 2013 Jul 1;8(7):e68665. doi: 10.1371/journal.pone.0068665. Print 2013. PLoS One. 2013. PMID: 23840900 Free PMC article. - DEAD-box protein DDX3 associates with eIF4F to promote translation of selected mRNAs.
Soto-Rifo R, Rubilar PS, Limousin T, de Breyne S, Décimo D, Ohlmann T. Soto-Rifo R, et al. EMBO J. 2012 Sep 12;31(18):3745-56. doi: 10.1038/emboj.2012.220. Epub 2012 Aug 7. EMBO J. 2012. PMID: 22872150 Free PMC article. - New function for the RNA helicase p68/DDX5 as a modifier of MBNL1 activity on expanded CUG repeats.
Laurent FX, Sureau A, Klein AF, Trouslard F, Gasnier E, Furling D, Marie J. Laurent FX, et al. Nucleic Acids Res. 2012 Apr;40(7):3159-71. doi: 10.1093/nar/gkr1228. Epub 2011 Dec 9. Nucleic Acids Res. 2012. PMID: 22156369 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Other Literature Sources