Structural Basis of DEAH/RHA Helicase Activity
AbstractDEAH/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
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Chen, M.C.; Ferré-D’Amaré, A.R. Structural Basis of DEAH/RHA Helicase Activity. Crystals 2017, 7, 253.
Chen MC, Ferré-D’Amaré AR. Structural Basis of DEAH/RHA Helicase Activity. Crystals. 2017; 7(8):253.Chicago/Turabian Style
Chen, Michael C.; Ferré-D’Amaré, Adrian R. 2017. "Structural Basis of DEAH/RHA Helicase Activity." Crystals 7, no. 8: 253.
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