Structural highlights
Function
[RHO_THEMA] Facilitates transcription termination by a mechanism that involves Rho binding to the nascent RNA, activation of Rho's RNA-dependent ATPase activity, and release of the mRNA from the DNA template.[HAMAP-Rule:MF_01884]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The Rho factor is a ring-shaped ATP-dependent helicase that mediates transcription termination in most prokaryotic cells by disengaging the transcription elongation complex formed by the RNA polymerase, DNA, and the nascent RNA transcript. The crystal structures of key intermediates along the kinetic pathway of RNA binding to Rho unveiled an unprecedented mode of helicase loading and provided a model for the ATP turnover coupled to coordinated strand movement. Here we report the structure of the early RNA-free state of Rho, which had eluded crystallization for many years but now completes the series. The structure allows the characterization of the apo-form Rho from Thermotoga maritima to 2.3 A resolution, reveals an RNA-recruiting site that becomes hidden after occupancy of the adjacent specific primary RNA-binding site, and suggests an enriched model for mRNA capture that is consistent with previous data.
The structure of RNA-free Rho termination factor indicates a dynamic mechanism of transcript capture.,Canals A, Uson I, Coll M J Mol Biol. 2010 Jul 2;400(1):16-23. Epub 2010 May 7. PMID:20452362[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Canals A, Uson I, Coll M. The structure of RNA-free Rho termination factor indicates a dynamic mechanism of transcript capture. J Mol Biol. 2010 Jul 2;400(1):16-23. Epub 2010 May 7. PMID:20452362 doi:10.1016/j.jmb.2010.05.004
