The DExH protein NPH-II is a processive and directional motor for unwinding RNA

Eckhard Jankowsky, Christian H. Gross, Stewart Shuman and Anna Marie Pyle
Additional contact information
Eckhard Jankowsky: Columbia University
Christian H. Gross: The Program in Molecular Biology, Sloan-Kettering Institute
Stewart Shuman: The Program in Molecular Biology, Sloan-Kettering Institute
Anna Marie Pyle: Columbia University

Nature, 2000, vol. 403, issue 6768, 447-451

Abstract: 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 fashion1. DExH/D proteins are also essential for the replication of many viruses, and therefore provide targets for the development of therapeutics2. All DExH/D proteins characterized to date hydrolyse nucleoside triphosphates and, in most cases, this activity is stimulated by the addition of RNA or DNA1. Several members of the family unwind RNA duplexes in an NTP-dependent fashion in vitro1,3; therefore it has been proposed that DExH/D proteins couple NTP hydrolysis to RNA conformational change in complex macromolecular assemblies4. 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.

Date: 2000
References: Add references at CitEc
Citations: View citations in EconPapers (1)

Downloads: (external link)
https://www.nature.com/articles/35000239 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:403:y:2000:i:6768:d:10.1038_35000239

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/35000239

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().