Journal
CRYSTALS
Volume 7, Issue 8, Pages -Publisher
MDPI AG
DOI: 10.3390/cryst7080253
Keywords
DEAH/RHA; DExH; helicase; MLE; Prp43p; DHX36; HCV NS3
Funding
- Cambridge Trust Studentship
- Intramural Program of the National Heart, Lung, and Blood Institute, NIH
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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.
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