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Science 9 March 2001: Vol. 291. no. 5510, pp. 1916 - 1917 DOI: 10.1126/science.1059682
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Perspectives
MOLECULAR BIOLOGY: RNP Remodeling With DExH/D Boxes
Cindy L. Will and Reinhard Lührmann
The DExH/D proteins are known to have RNA helicase activity, that is, they bind to and unwind double-stranded RNA. As Will and Lührmann explain in their Perspective, these enzymes can also behave as RNPases, disrupting the interactions between RNA and proteins in ribonucleoprotein complexes such as the spliceosome.
The authors are in the Cellular Biochemistry Department, Max Planck Institute for Biophysical Chemistry, Am Fassberg 11, 37077 Göttingen, Germany. E-mail: cwill1{at}gwdg.de; reinhard.luehrmann{at}mpi-bpc.mpg.de
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- ATPase/Helicase Activities of p68 RNA Helicase Are Required for Pre-mRNA Splicing but Not for Assembly of the Spliceosome.
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- Protein Displacement by DExH/D "RNA Helicases" Without Duplex Unwinding.
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- Ded1p, a conserved DExD/H-box translation factor, can promote yeast L-A virus negative-strand RNA synthesis in vitro.
- J.-L. Chong, R.-Y. Chuang, L. Tung, and T.-H. Chang (2004)
Nucleic Acids Res.
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- Splicing enhances translation in mammalian cells: an additional function of the exon junction complex.
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- Regulation of Alternative Splicing by the ATP-Dependent DEAD-Box RNA Helicase p72.
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- p68 RNA Helicase Is an Essential Human Splicing Factor That Acts at the U1 snRNA-5' Splice Site Duplex.
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- Probing Interactions between the U2 Small Nuclear Ribonucleoprotein and the DEAD-box Protein, Prp5.
- B. K. Abu Dayyeh, T. K. Quan, M. Castro, and S. W. Ruby (2002)
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