Structure of the Rho Transcription Terminator Mechanism of mRNA Recognition and Helicase Loading

  title={Structure of the Rho Transcription Terminator Mechanism of mRNA Recognition and Helicase Loading},
  author={Emmanuel Skordalakes and James M. Berger},

Figures and Tables from this paper

Getting a grip on the terminator.
Rho-dependent transcription termination: more questions than answers.
This review has attempted to summarize "the knowns" and "the unknowns" of the Rho protein revealed by the recent developments in this field.
The RNA-mediated, asymmetric ring regulatory mechanism of the transcription termination Rho helicase decrypted by time-resolved Nucleotide Analog Interference Probing (trNAIP)
A new combinatorial approach, called time-resolved Nucleotide Analog Interference Probing (trNAIP), is developed and used to unmask RNA molecular determinants of catalytic Rho function, identifying a regulatory step in the translocation cycle involving recruitment of the 2′-hydroxyl group of the incoming 3′-RNA nucleotide by a Rho subunit.


The structural basis for terminator recognition by the Rho transcription termination factor.
A physical model for the translocation and helicase activities of Escherichia coli transcription termination protein Rho.
It is proposed that the quaternary structure of Rho coordinates the ATP-driven RNA binding and release processes to produce a biased random walk of the Rho hexamer along the RNA, followed by RNA.
Three-dimensional reconstruction of transcription termination factor rho: orientation of the N-terminal domain and visualization of an RNA-binding site.
A three-dimensional reconstruction of rho is generated, and a tRNA molecule bound to the primary RNA-binding site to the outside of the ring is localized.
Rho-dependent termination and ATPases in transcript termination.
Rho and RNA: models for recognition and response
  • T. Platt
  • Biology
    Molecular microbiology
  • 1994
New insights are offered into the requirements for binding and ATPase activation by a variety of RNA substrates, dynamic analyses of Rho tracking, helicase and termination activity, and the participation of a new factor (NusG) that interacts with Rho.
Transcription termination factor rho is an RNA-DNA helicase
ATP and other nucleotides stabilize the Rho-mRNA complex.
The experimental evidence indicates that the hexameric form of Rho is stabilized slightly by binding to a transcript but that the protein on RNA is in equilibrium with nonhexameric forms, suggesting that a Rho hexamer can form on a transcript by addition of subunits to a partial assembly.
Transcription Factor Rho Does Not Require a Free End to Act as an RNA-DNA Helicase on an RNA*
The action of Rho on a transcript does not depend on the availability of a free 5′ terminus, and Rho bound nearly as tightly to the circular derivative RNA as to the standardcro transcript.
RNA sequence and secondary structure requirements for rho-dependent transcription termination.
The results of the sequence comparisons reported here strongly support the generality of the "unstructured binding site" hypothesis for rho-dependent termination.
RNA Passes through the Hole of the Protein Hexamer in the Complex with the Escherichia coli Rho Factor*
Results from the cross-linking of the modified Rho proteins to a series of λ cro RNA derivatives showed that Cys-82 Rho formed cross-links with all transcripts containing the Rho utilization (rut) site, and that CYS-325 Rhoformed cross- links to transcripts that had therut site and 10 or more residues 3′ of the rut site.