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

Allosteric control of catalysis by the F loop of RNA polymerase.

Proceedings of the National Academy of Sciences of the United States of America - 10 Nov 2009

Miropolskaya Nataliya, Artsimovitch Irina, Klimasauskas Saulius, Nikiforov Vadim, Kulbachinskiy Andrey

Abstract excerpt

Bacterial RNA polymerases (RNAPs) undergo coordinated conformational changes during catalysis. In particular, concerted folding of the trigger loop and rearrangements of the bridge helix at the RNAP active center have been implicated in nucleotide addition and RNAP translocation. At moderate temperatures, the rate of catalysis by RNAP from thermophilic Thermus aquaticus is dramatically reduced compared with its...

Read the complete abstract on PubMed

Topics

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

Share to Aminoglycosides
Share to Catalysis

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Allosteric Regulation

Share to Deinococcus

Share to DNA-Directed RNA Polymerases

Share to Drug Resistance

Share to Protein Folding

Share to Thermus

Source

Open in PubMed Open full text

Identifiers

PMID: 19855007
DOI: 10.1073/pnas.0905402106
PMCID: PMC2776430

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Allosteric control of catalysis by the F loop of RNA polymerase.PMID 19855007Read ↗

Interplay between the trigger loop and the F loop during RNA polymerase catalysis.Semantic proximity Read ↗

Insights into the regulatory function of the ɛ subunit from bacterial F-type ATP synthases: a comparison of structural, biochemical and biophysical data.Semantic proximity Read ↗

Conserved functions of the trigger loop and Gre factors in RNA cleavage by bacterial RNA polymerases.Semantic proximity Read ↗

Mutations in RNA Polymerase Bridge Helix and Switch Regions Affect Active-Site Networks and Transcript-Assisted Hydrolysis.Semantic proximity Read ↗

Modulation of RNA polymerase activity through the trigger loop folding.Semantic proximity Read ↗

Activity map of the Escherichia coli RNA polymerase bridge helix.Semantic proximity Read ↗

Comparative study on tertiary contacts and folding of RNase P RNAs from a psychrophilic, a mesophilic/radiation-resistant, and a thermophilic bacterium.Semantic proximity Read ↗

Structural perspective on mutations affecting the function of multisubunit RNA polymerases.Semantic proximity Read ↗

The role of the bacterial RNA polymerase beta subunit flexible flap domain in transcription termination.Semantic proximity Read ↗

A bridge to transcription by RNA polymerase.Semantic proximity Read ↗

Conformational coupling, bridge helix dynamics and active site dehydration in catalysis by RNA polymerase.Semantic proximity Read ↗

Lineage-specific variations in the trigger loop modulate RNA proofreading by bacterial RNA polymerases.Semantic proximity Read ↗

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