Structure of the Rho transcription terminator: Mechanism of mRNA recognition and helicase loading

Emmanuel Skordalakes, James M. Berger

Research output: Contribution to journalArticlepeer-review

Abstract

In bacteria, one of the major transcriptional termination mechanisms requires a RNA/DNA helicase known as the Rho factor. We have determined two structures of Rho complexed with nucleic acid recognition site mimics in both free and nucleotide bound states to 3.0 Å resolution. Both structures show that Rho forms a hexameric ring in which two RNA binding sites - a primary one responsible for target mRNA recognition and a secondary one required for mRNA translocation and unwinding - point toward the center of the ring. Rather than forming a closed ring, the Rho hexamer is split open, resembling a "lock washer" in its global architecture. The distance between subunits at the opening is sufficiently wide (12 Å) to accommodate single-stranded RNA. This open configuration most likely resembles a state poised to load onto mRNA and suggests how related ring-shaped enzymes may be breached to bind nucleic acids.

Original languageEnglish (US)
Pages (from-to)135-146
Number of pages12
JournalCell
Volume114
Issue number1
DOIs
StatePublished - Jul 11 2003
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)

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