Interaction of the Escherichia coli DEAD box protein DbpA with 23 S ribosomal RNA

G. E. Pugh, S. M. Nicol, F. V. Fuller-Pace (Lead / Corresponding author)

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    42 Citations (Scopus)


    The Escherichia coli DEAD box protein DbpA is unique among the DEAD box family in that its ATPase activity is specifically stimulated by bacterial 23 S ribosomal RNA. We have analysed the interaction between DbpA and a specific region within 23 S rRNA (namely nucleotides 2508-2580) which stimulates full ATPase activity. Using electrophoretic mobility shift assays we show that DbpA binds to this 'specific' region with greater efficiency than to other regions of 23 S rRNA, and is not competed off by a non-specific RNA or a mutant RNA in which one of the stem-loops has been disrupted. These data suggest that the secondary structure within this region of 23 S rRNA is important for its recognition and binding by DbpA. We have also examined the ability of DbpA to unwind RNA and show that the purified protein does not behave as an RNA helicase in vitro with the substrates tested.

    Original languageEnglish
    Pages (from-to)771-778
    Number of pages8
    JournalJournal of Molecular Biology
    Issue number4
    Publication statusPublished - 1 Oct 1999


    • 23 S rRNA
    • ATPase
    • DbpA
    • DEAD-box protein
    • RNA binding


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