ATP hydrolysis is required for DEAD-box protein recycling but not for duplex unwinding

Fei Liu, Andrea Putnam, Eckhard Jankowsky

Research output: Contribution to journalArticlepeer-review

Abstract

DEAD-box proteins, the largest helicase family, catalyze ATP-dependent remodeling of RNA-protein complexes and the unwinding of RNA duplexes. Because DEAD-box proteins hydrolyze ATP in an RNA-dependent fashion, the energy provided by ATP hydrolysis is commonly assumed to drive the energetically unfavorable duplex unwinding. Here, we show efficient unwinding of stable duplexes by several DEAD-box proteins in the presence of the nonhydrolyzable ATP analog ADP-beryllium fluoride. Another ATP analog, ADP-aluminum fluoride, does not promote unwinding. The findings show that the energy from ATP hydrolysis is dispensable for strand separation. ATP binding, however, appears necessary. ATP hydrolysis is found to be required for fast enzyme release from the RNA and multiple substrate turnovers and thus for enzyme recycling.

Original languageEnglish (US)
Pages (from-to)20209-20214
Number of pages6
JournalProceedings of the National Academy of Sciences of the United States of America
Volume105
Issue number51
DOIs
StatePublished - Dec 23 2008
Externally publishedYes

Keywords

  • Ded1
  • Helicase
  • Mss116
  • RNA
  • eIF4A

ASJC Scopus subject areas

  • General

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