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Science 9 March 2001:
Vol. 291. no. 5510, pp. 1916 - 1917
DOI: 10.1126/science.1059682

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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The network of protein-protein interactions within the human U4/U6.U5 tri-snRNP.
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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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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.
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