Next Article in Journal
Mechanical Anisotropy in Austenitic NiMnGa Alloy: Nanoindentation Studies
Previous Article in Journal
Interfacial Kinetics of Efficient Perovskite Solar Cells
Previous Article in Special Issue
Phosphorus SAD Phasing for Nucleic Acid Structures: Limitations and Potential
Article Menu
Issue 8 (August) cover image

Export Article

Open AccessReview
Crystals 2017, 7(8), 253; doi:10.3390/cryst7080253

Structural Basis of DEAH/RHA Helicase Activity

1
Biochemistry and Biophysics Center, National Heart, Lung and Blood Institute, Bethesda, MD 20892, USA
2
Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, UK
*
Author to whom correspondence should be addressed.
Academic Editor: Jinwei Zhang
Received: 6 July 2017 / Revised: 12 August 2017 / Accepted: 13 August 2017 / Published: 15 August 2017
(This article belongs to the Special Issue Nucleic Acid Crystallography)
View Full-Text   |   Download PDF [21528 KB, uploaded 16 August 2017]   |  

Abstract

DEAH/RHA helicases are members of a large group of proteins collectively termed DExH-box, which also include Ski2-like and NS3/NPH-II helicases. By binding and remodeling DNA and RNA, DEAH/RHA helicases play critical roles in many cellular processes ranging from transcription and splicing to ribosome biogenesis, innate immunity and stress granule formation. While numerous crystal structures of other DExH-box proteins helicases have been reported, no structures of DEAH/RHA helicases bound to nucleic acid substrates have been available until the recent co-crystal structures of the maleless (MLE) and Prp43p bound to RNA. This review examines how these new structures provide a starting point to understand how DEAH/RHA helicases bind to, translocate on, and unwind nucleic acid substrates. View Full-Text
Keywords: DEAH/RHA; DExH; helicase; MLE; Prp43p; DHX36; HCV NS3 DEAH/RHA; DExH; helicase; MLE; Prp43p; DHX36; HCV NS3
Figures

Figure 1

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).

Scifeed alert for new publications

Never miss any articles matching your research from any publisher
  • Get alerts for new papers matching your research
  • Find out the new papers from selected authors
  • Updated daily for 49'000+ journals and 6000+ publishers
  • Define your Scifeed now

SciFeed Share & Cite This Article

MDPI and ACS Style

Chen, M.C.; Ferré-D’Amaré, A.R. Structural Basis of DEAH/RHA Helicase Activity. Crystals 2017, 7, 253.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Crystals EISSN 2073-4352 Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top