The Rho termination factor disengages newly transcribed RNA from its DNA template at certain, specific transcripts. It it thought that two copies of Rho bind to RNA and that Rho functions as a hexamer of protomers (PUBMED:10230401). This domain is found to the N-terminus of the RNA binding domain.
The Rho termination factor disengages newly transcribed RNA from its DNA template at certain, specific transcripts. It is thought that two copies of Rho bind to RNA and that Rho functions as a hexamer of protomers [ (PUBMED:10230401) ]. This domain is found to the N terminus of the RNA binding domain ( IPR011113 ).
The structural basis for terminator recognition by the Rho transcriptiontermination factor.
Mol Cell. 1999; 3: 487-93
Display abstract
The E. coli Rho protein disengages newly transcribed RNA from its DNAtemplate, helping terminate certain transcripts. We have determined theX-ray crystal structure of the RNA-binding domain of Rho complexed to anRNA ligand. Filters that screen both ligand size and chemicalfunctionality line the primary nucleic acid-binding site, impartingsequence specificity to a generic single-stranded nucleic acid-bindingfold and explaining the preference of Rho for cytosine-rich RNA. Thecrystal packing reveals two Rho domain protomers bound to a single RNAwith a single base spacer, suggesting that the strong RNA-binding sites ofRho may arise from pairing of RNA-binding modules. Dimerization ofsymmetric subunits on an asymmetric ligand is developed as a model forallosteric control in the action of the intact Rho hexamer.
Structural mechanism of inhibition of the Rho transcription termination factor by the antibiotic 5a-(3-formylphenylsulfanyl)-dihydrobicyclomycin (FPDB)
