Escherichia coli DbpA is an RNA helicase that requires hairpin 92 of 23S rRNA

C. M. Diges, O. C. Uhlenbeck

Research output: Contribution to journalArticlepeer-review

113 Scopus citations

Abstract

Escherichia coli DbpA is a member of the DEAD/H family of proteins which has been shown to have robust ATPase activity only in the presence of a specific region of 23S rRNA. A series of bimolecular RNA substrates were designed based on this activating region of rRNA and used to demonstrate that DbpA is also a non-processive, sequence-specific RNA helicase. The high affinity of DbpA for the RNA substrates allowed both single and multiple turnover helicase assays to be performed. Helicase activity of DbpA is dependent on the presence of ATP or dATP, the sequence of the loop of hairpin 92 of 23S rRNA and the position of the substrate helix with respect to hairpin 92. This work indicates that certain RNA helicases require particular RNA structures in order for optimal unwinding activity to be observed.

Original languageEnglish (US)
Pages (from-to)5503-5512
Number of pages10
JournalEMBO Journal
Volume20
Issue number19
DOIs
StatePublished - Oct 1 2001

Keywords

  • E.coli 23S rRNA
  • Processivity
  • RNA-binding protein

ASJC Scopus subject areas

  • Neuroscience(all)
  • Molecular Biology
  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)

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