The structural basis for terminator recognition by the Rho transcription termination factor

Cynthia E. Bogden, Deborah Fass, Nick Bergman, Matthew D. Nichols, James M Berger

Research output: Contribution to journalArticle

Abstract

The E. coli Rho protein disengages newly transcribed RNA from its DNA template, helping terminate certain transcripts. We have determined the X- ray crystal structure of the RNA-binding domain of Rho complexed to an RNA ligand. Filters that screen both ligand size and chemical functionality line the primary nucleic acid-binding site, imparting sequence specificity to a generic single-stranded nucleic acid-binding fold and explaining the preference of Rho for cytosine-rich RNA. The crystal packing reveals two Rho domain protomers bound to a single RNA with a single base spacer, suggesting that the strong RNA-binding sites of Rho may arise from pairing of RNA- binding modules. Dimerization of symmetric subunits on an asymmetric ligand is developed as a model for allosteric control in the action of the intact Rho hexamer.

Original languageEnglish (US)
Pages (from-to)487-493
Number of pages7
JournalMolecular Cell
Volume3
Issue number4
DOIs
StatePublished - Apr 1999
Externally publishedYes

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Transcription Factors
RNA
Ligands
Nucleic Acids
Binding Sites
Cytosine
Protein Subunits
Dimerization
X-Rays
DNA

ASJC Scopus subject areas

  • Molecular Biology

Cite this

The structural basis for terminator recognition by the Rho transcription termination factor. / Bogden, Cynthia E.; Fass, Deborah; Bergman, Nick; Nichols, Matthew D.; Berger, James M.

In: Molecular Cell, Vol. 3, No. 4, 04.1999, p. 487-493.

Research output: Contribution to journalArticle

Bogden, Cynthia E. ; Fass, Deborah ; Bergman, Nick ; Nichols, Matthew D. ; Berger, James M. / The structural basis for terminator recognition by the Rho transcription termination factor. In: Molecular Cell. 1999 ; Vol. 3, No. 4. pp. 487-493.
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