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Rho-dependent termination and ATPases in transcript termination.

John P Richardson1

  • 1Department of Chemistry, Indiana University, 800 East Kirkwood Avenue, Bloomington, IN 47405, USA. richardj@indiana.edu

Biochimica Et Biophysica Acta
|September 6, 2002
PubMed
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Transcription factor Rho, a ring-shaped protein, terminates RNA synthesis by binding nascent RNA and using ATP hydrolysis to pull the transcript from RNA polymerase. This process involves specific RNA-binding and ATP-binding domains.

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Genetics

Background:

  • Transcription factor Rho is a homohexameric protein crucial for transcript termination.
  • Rho possesses a distinct RNA-binding domain (RNA-BD) and a proposed ATP-binding domain (ATP-BD).

Purpose of the Study:

  • To propose a model for Rho-mediated transcript termination.
  • To elucidate the mechanism of Rho's interaction with nascent RNA and RNA polymerase.

Main Methods:

  • Homology modeling was used to propose the structure of the ATP-binding domain.
  • A mechanistic model was developed based on existing structural and functional data.

Main Results:

  • Rho interacts with a C-rich rut region on nascent RNA emerging from RNA polymerase.

Related Experiment Videos

  • A subunit release mechanism allows the 3' RNA segment into Rho's central channel.
  • ATP hydrolysis drives the pulling of RNA, leading to transcript termination.

    • Conclusions:

    • The proposed model details Rho's hexameric action in transcript termination.
    • Rho utilizes ATP hydrolysis to disengage nascent RNA from the transcription machinery.
    • Understanding Rho's mechanism provides insight into bacterial gene regulation.