PMID:10873452
| Citation |
Yu, X, Horiguchi, T, Shigesada, K and Egelman, EH (2000) Three-dimensional reconstruction of transcription termination factor rho: orientation of the N-terminal domain and visualization of an RNA-binding site. J. Mol. Biol. 299:1279-87 |
|---|---|
| Abstract |
The Escherichia coli rho transcription termination protein is a hexameric helicase, and is believed to function by separating an RNA-DNA hybrid. Unlike hexameric DNA helicases, where a single strand of DNA passes through the central channel, it has been proposed that the RNA wraps around the outside of the ring. We have generated a three-dimensional reconstruction of rho, and localized a tRNA molecule bound to the primary RNA-binding site to the outside of the ring. An atomic structure of the N-terminal domain of rho fits into our reconstruction uniquely, with the residues involved in RNA-binding on the outside of the ring. Although rho shares a common structural core with the F1-ATPase and other hexameric helicases, there has been a divergence in function due to rho's N-terminal domain, which has no homology to other helicases. |
| Links |
PubMed Online version:10.1006/jmbi.2000.3810 |
| Keywords |
Binding Sites; Escherichia coli/chemistry; Escherichia coli/genetics; Microscopy, Electron; Models, Biological; Models, Molecular; Protein Structure, Quaternary; Protein Structure, Secondary; Proton-Translocating ATPases/chemistry; Proton-Translocating ATPases/ultrastructure; RNA, Bacterial/genetics; RNA, Bacterial/metabolism; RNA, Transfer/genetics; RNA, Transfer/metabolism; RNA-Binding Proteins/chemistry; RNA-Binding Proteins/metabolism; RNA-Binding Proteins/ultrastructure; Rho Factor/chemistry; Rho Factor/metabolism; Rho Factor/ultrastructure; Transcription, Genetic/genetics |
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