Division of Labor in an Oligomer of the DEAD-Box RNA Helicase Ded1p

Andrea A. Putnam, Zhaofeng Gao, Fei Liu, Huijue Jia, Quansheng Yang, Eckhard Jankowsky

Research output: Contribution to journalArticlepeer-review

Abstract

Most aspects of RNA metabolism involve DEAD-box RNA helicases, enzymes that bind and remodel RNA and RNA-protein complexes in an ATP-dependent manner. Here we show that the DEAD-box helicase Ded1p oligomerizes in the cell and in vitro, and unwinds RNA as a trimer. Two protomers bind the single-stranded region of RNA substrates and load a third protomer to the duplex which then separates the strands. ATP utilization differs between the strand-separating protomer and those bound to the single-stranded region. Binding of the eukaryotic initiation factor 4G to Ded1p interferes with oligomerization and thereby modulates unwinding activity and RNA affinity of the helicase. Our data reveal a strict division of labor between the Ded1p protomers in the oligomer. This mode of oligomerization fundamentally differs from other helicases. Oligomerization represents a previously unappreciated level of regulation for DEAD-box helicase activities.

Original languageEnglish (US)
Pages (from-to)541-552
Number of pages12
JournalMolecular cell
Volume59
Issue number4
DOIs
StatePublished - Aug 20 2015
Externally publishedYes

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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