Nucleic Acids Research Advance Access originally published online on August 25, 2006
Nucleic Acids Research 2006 34(15):4181-4188; doi:10.1093/nar/gkl410
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Nucleic Acids Research, 2006, Vol. 34, No. 15 4181-4188
© 2006 The Author(s)
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
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Remodeling of ribonucleoprotein complexes with DExH/D RNA helicases
Department of Biochemistry, Center for RNA Molecular Biology, Wood W447, School of Medicine Case Western Reserve University, 10900 Euclid Avenue Cleveland, OH 44122, USA
*To whom correspondence should be addressed. Tel: +1 216 368 3336; Fax: + 1 216 368 3336; Email: exj13{at}case.edu
Received March 24, 2006. Revised May 10, 2006. Accepted May 17, 2006.
The DExH/D protein family is the largest group of enzymes in eukaryotic RNA metabolism. DExH/D proteins are mainly known for their ability to unwind RNA duplexes in an ATP-dependent fashion. However, it has become clear in recent years that these DExH/D RNA helicases are also involved in the ATP-dependent remodeling of RNA–protein complexes. Here we review recent studies that highlight physiological roles of DExH/D proteins in the displacement of proteins from RNA. We further discuss work with simple RNA–protein complexes in vitro, which illuminates mechanisms by which DExH/D proteins remove proteins from RNA. Although we are only beginning to understand how DExH/D proteins remodel RNA–protein complexes, these studies have shown that an ‘RNA helicase’ does not per se require cofactors to displace proteins from RNA, that protein displacement does not necessarily involve RNA duplex unwinding, and that not all DExH/D proteins are able to disassemble the same range of ribonucleoproteins.
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