PMID:10230401
| Citation |
Bogden, CE, Fass, D, Bergman, N, Nichols, MD and Berger, JM (1999) The structural basis for terminator recognition by the Rho transcription termination factor. Mol. Cell 3:487-93 |
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| 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. |
| Links | |
| Keywords |
Allosteric Regulation/genetics; Crystallography, X-Ray; Escherichia coli/genetics; Hydrogen Bonding; Models, Molecular; Molecular Sequence Data; Nucleic Acid Conformation; Protein Conformation; RNA/chemistry; RNA-Binding Proteins/chemistry; Rho Factor/chemistry |
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