DEAD-box proteins: the driving forces behind RNA metabolism
Top Cited Papers
- 1 March 2004
- journal article
- review article
- Published by Springer Science and Business Media LLC in Nature Reviews Molecular Cell Biology
- Vol. 5 (3), 232-241
- https://doi.org/10.1038/nrm1335
Abstract
RNA helicases of the DEAD-box protein family all have nine characteristic motifs. These motifs clearly distinguish this family from other, highly related, RNA helicase families such as the DEAH-box or the Ski2 families. The motifs are contained within a core domain that is flanked by less-conserved regions, which are likely to represent specificity elements for substrate targeting, interaction with other proteins or cellular localization. RNA helicases of the DEAD-box family are required for different cellular processes such as transcription, pre-mRNA processing, ribosome biogenesis, nuclear mRNA export, translation initiation, RNA turnover and organelle function. The structure of the core element, which contains all the conserved motifs that are required for helicase activity, is very similar to viral RNA helicases and to DNA helicases, which indicates that the fundamental activities of these enzymes are similar. ATP-binding and hydrolysis by the core element induce conformational changes that are responsible for the enzymatic activity of these proteins; that is, unwinding of duplex RNA or disrupting RNA–protein complexes. The enzymatic activity varies among different proteins and can be more or less processive, parameters that are probably influenced by interacting partners and the substrate.Keywords
This publication has 103 references indexed in Scilit:
- Synergism between p68 RNA helicase and the transcriptional coactivators CBP and p300Oncogene, 2003
- The SWISS-PROT protein knowledgebase and its supplement TrEMBL in 2003Nucleic Acids Research, 2003
- The Carboxy-terminal Domain of the DEx Protein YxiN is Sufficient to Confer Specificity for 23S rRNAJournal of Molecular Biology, 2002
- An extensive network of coupling among gene expression machinesNature, 2002
- The requirement for eukaryotic initiation factor 4A (eIF4A) in translation is in direct proportion to the degree of mRNA 5′ secondary structureRNA, 2001
- Low temperature regulated DEAD-box RNA helicase from the antarctic archaeon, Methanococcoides burtoniiJournal of Molecular Biology, 2000
- The 3' to 5' degradation of yeast mRNAs is a general mechanism for mRNA turnover that requires the SKI2 DEVH box protein and 3' to 5' exonucleases of the exosome complexThe EMBO Journal, 1998
- Crystal structure of a DExx box DNA helicaseNature, 1996
- Helicases: amino acid sequence comparisons and structure-function relationshipsCurrent Opinion in Structural Biology, 1993
- RNA helicase activity associated with the human p68 proteinNature, 1989