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

Expression, abundance, and RNA polymerase binding properties of the delta factor of Bacillus subtilis.

The Journal of biological chemistry - 28 May 1999

López de Saro F J, Yoshikawa N, Helmann J D

Abstract excerpt

The delta protein is a dispensable subunit of Bacillus subtilis RNA polymerase (RNAP) that has major effects on the biochemical properties of the purified enzyme. In the presence of delta, RNAP displays an increased specificity of transcription, a decreased affinity for nucleic acids, and an incr...

Read the complete abstract on PubMed

Topics

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

Share to Bacillus subtilis
Share to Cell Division
Share to Cyclic AMP-Dependent Protein Kinases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to DNA-Directed RNA Polymerases

Share to Erythroid-Specific DNA-Binding Factors

Share to Gene Expression Regulation, Bacterial

Share to Genes, Reporter

Share to Sigma Factor

Source

Identifiers

PMID: 10336502
DOI: 10.1074/jbc.274.22.15953

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026. Prepared record publication-10336502-2026-09-01.1. Manifest publication-graph-cohort-2026-09-01.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 1 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Expression, abundance, and RNA polymerase binding properties of the delta factor of Bacillus subtilis.PMID 10336502Read ↗

Phenotypic characterization and complementation analysis of Bacillus subtilis 6S RNA single and double deletion mutants.Semantic proximity Read ↗

Characterization of HelD, an interacting partner of RNA polymerase from Bacillus subtilis.Semantic proximity Read ↗

Pleiotropic roles of elongation factor P in Bacillus subtilis physiology revealed by phenotypic and multi-omics analyses.Semantic proximity Read ↗

Loss of the Rpb4/Rpb7 subcomplex in a mutant form of the Rpb6 subunit shared by RNA polymerases I, II, and III.Semantic proximity Read ↗

A highly conserved 6S RNA structure is required for regulation of transcription.Semantic proximity Read ↗

Transcription factor GreA contributes to resolving promoter-proximal pausing of RNA polymerase in Bacillus subtilis cells.Semantic proximity Read ↗

Archaeal RNA polymerase subunits E and F are not required for transcription in vitro, but a Thermococcus kodakarensis mutant lacking subunit F is temperature-sensitive.Semantic proximity Read ↗

Characterization of a novel RNA polymerase mutant that alters DksA activity.Semantic proximity Read ↗

Tracking the Elusive Function of Bacillus subtilis Hfq.Semantic proximity Read ↗

Identifying interacting regions in the beta subunit of Escherichia coli RNA polymerase.Semantic proximity Read ↗

Structural and functional characterization of partner switching regulating the environmental stress response in Bacillus subtilis.Semantic proximity Read ↗

Temporal and selective association of multiple sigma factors with RNA polymerase during sporulation in Bacillus subtilis.Semantic proximity Read ↗

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