The DExH protein NPH-II is a processive and directional motor for unwinding RNA Journal Article
| Authors: | Jankowsky, E.; Gross, C. H.; Shuman, S.; Pyle, A. M. |
| Article Title: | The DExH protein NPH-II is a processive and directional motor for unwinding RNA |
| Abstract: | All aspects of cellular RNA metabolism and processing involve DExH/D proteins, which are a family of enzymes that unwind or manipulate RNA in an ATP-dependent fashion. DExH/D proteins are also essential for the replication of many viruses, and therefore provide targets for the development of therapeutics. All DExH/D proteins characterized to date hydrolyse nucleoside triphosphates and, in most cases, this activity is stimulated by the addition of RNA or DNA. Several members of the family unwind RNA duplexes in an NTP- dependent fashion in vitro; therefore it has been proposed that DExH/D proteins couple NTP hydrolysis to RNA conformational change in complex macromolecular assemblies. Despite the central role of DExH/D proteins, their mechanism of RNA helicase activity remains unknown. Here we show that the DExH protein NPH-II unwinds RNA duplexes in a processive, unidirectional fashion with a step size of roughly one-half helix turn. We show that there is a quantitative connection between ATP utilization and helicase processivity, thereby providing direct evidence that DExH/D proteins can function as molecular motors on RNA. |
| Keywords: | protein expression; unclassified drug; enzyme activity; rna; kinetics; vaccinia virus; virus replication; protein family; rna processing; rna helicase; rna helicases; rna metabolism; rna degradation; deoxycytidine kinase; molecular motor proteins; priority journal; article; dexh protein; nph ii protein |
| Journal Title: | Nature |
| Volume: | 403 |
| Issue: | 6768 |
| ISSN: | 0028-0836 |
| Publisher: | Nature Publishing Group |
| Date Published: | 2000-01-27 |
| Start Page: | 447 |
| End Page: | 451 |
| Language: | English |
| DOI: | 10.1038/35000239 |
| PUBMED: | 10667799 |
| PROVIDER: | scopus |
| DOI/URL: | |
| Notes: | Export Date: 18 November 2015 -- Source: Scopus |
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