Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Mechanochemistry of transcription termination factor Rho.

Molecular cell - 9 Jun 2006

Adelman Joshua L, Jeong Yong-Joo, Liao Jung-Chi, Patel Gayatri, Kim Dong-Eun, Oster George, Patel Smita S

Abstract excerpt

Rho is a ring-shaped hexameric motor protein that translocates along nascent mRNA transcript and terminates transcription of select genes in bacteria. Using a numerical optimization algorithm that simultaneously fits all of the presteady-state ATPase kinetic data, we determine how Rho utilizes the chemical energy of ATP hydrolysis to translocate RNA. A random hydrolysis mechanism is ruled out by the observed...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Hydrolysis
Share to Nucleotides
Share to Adenosine Triphosphate

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Phosphates

Share to Protein Subunits

Share to Rho Factor

Share to Terminator Regions, Genetic

Share to Translocation, Genetic

Source

Identifiers

PMID: 16762834
DOI: 10.1016/j.molcel.2006.04.022

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mechanochemistry of transcription termination factor Rho.PMID 16762834Read ↗

Mutagenesis-based evidence for an asymmetric configuration of the ring-shaped transcription termination factor Rho.Semantic proximity Read ↗

Transcription termination defective mutants of Rho: role of different functions of Rho in releasing RNA from the elongation complex.Semantic proximity Read ↗

Mutations in the rho transcription termination factor that affect RNA tracking.Semantic proximity Read ↗

An allosteric mechanism of Rho-dependent transcription termination.Semantic proximity Read ↗

Mutations in the ATP-binding domain of Escherichia coli rho factor affect transcription termination in vivo.Semantic proximity Read ↗

ATP binding to Rho transcription termination factor. Mutant F355W ATP-induced fluorescence quenching reveals dynamic ATP binding.Semantic proximity Read ↗

A ratchet mechanism of transcription elongation and its control.Semantic proximity Read ↗

Structural mechanism of inhibition of the Rho transcription termination factor by the antibiotic bicyclomycin.Semantic proximity Read ↗

Redundancy of primary RNA-binding functions of the bacterial transcription terminator Rho.Semantic proximity Read ↗

Mutational changes of conserved residues in the Q-loop region of transcription factor Rho greatly reduce secondary site RNA-binding.Semantic proximity Read ↗

Mutations in an RNP1 consensus sequence of Rho protein reduce RNA binding affinity but facilitate helicase turnover.Semantic proximity Read ↗

Analysis of E. coli rho factor: mutations affecting secondary-site interactions.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.