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Remodeling of ribonucleoprotein complexes with DExH/D RNA helicases
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-dep...
Autores principales: | , |
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Formato: | Texto |
Lenguaje: | English |
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Oxford University Press
2006
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1616955/ https://www.ncbi.nlm.nih.gov/pubmed/16935886 http://dx.doi.org/10.1093/nar/gkl410 |
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author | Jankowsky, Eckhard Bowers, Heath |
author_facet | Jankowsky, Eckhard Bowers, Heath |
author_sort | Jankowsky, Eckhard |
collection | PubMed |
description | 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. |
format | Text |
id | pubmed-1616955 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2006 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-16169552006-10-27 Remodeling of ribonucleoprotein complexes with DExH/D RNA helicases Jankowsky, Eckhard Bowers, Heath Nucleic Acids Res Survey and Summary 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. Oxford University Press 2006-09 2006-08-25 /pmc/articles/PMC1616955/ /pubmed/16935886 http://dx.doi.org/10.1093/nar/gkl410 Text en © 2006 The Author(s) |
spellingShingle | Survey and Summary Jankowsky, Eckhard Bowers, Heath Remodeling of ribonucleoprotein complexes with DExH/D RNA helicases |
title | Remodeling of ribonucleoprotein complexes with DExH/D RNA helicases |
title_full | Remodeling of ribonucleoprotein complexes with DExH/D RNA helicases |
title_fullStr | Remodeling of ribonucleoprotein complexes with DExH/D RNA helicases |
title_full_unstemmed | Remodeling of ribonucleoprotein complexes with DExH/D RNA helicases |
title_short | Remodeling of ribonucleoprotein complexes with DExH/D RNA helicases |
title_sort | remodeling of ribonucleoprotein complexes with dexh/d rna helicases |
topic | Survey and Summary |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1616955/ https://www.ncbi.nlm.nih.gov/pubmed/16935886 http://dx.doi.org/10.1093/nar/gkl410 |
work_keys_str_mv | AT jankowskyeckhard remodelingofribonucleoproteincomplexeswithdexhdrnahelicases AT bowersheath remodelingofribonucleoproteincomplexeswithdexhdrnahelicases |