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Protein Displacement by DExH/D "RNA Helicases" Without Duplex Unwinding

  • Margaret E. Fairman
  • , Patricia A. Maroney
  • , Wen Wang
  • , Heath A. Bowers
  • , Paul Gollnick
  • , Timothy W. Nilsen
  • , Eckhard Jankowsy
  • Case Western Reserve University

Research output: Contribution to journalArticlepeer-review

215 Scopus citations

Abstract

Members of the DExH/D superfamily of nucleic acid-activated nucleotide triphosphatases are essential for virtually all aspects of RNA metabolism, including pre-messenger RNA splicing, RNA interference, translation, and nucleocytoplasmic trafficking. Physiological substrates for these enzymes are thought to be regions of double-stranded RNA, because several DExH/D proteins catalyze strand separation in vitro. These "RNA helicases" can also disrupt RNA-protein interactions, but it is unclear whether this activity is coupled to duplex unwinding. Here we demonstrate that two unrelated DExH/D proteins catalyze protein displacement independently of duplex unwinding. Therefore, the essential functions of DExH/D proteins are not confined to RNA duplexes but can be exerted on a wide range of ribonucleoprotein substrates.

Original languageEnglish
Pages (from-to)730-734
Number of pages5
JournalScience
Volume304
Issue number5671
DOIs
StatePublished - Apr 30 2004

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