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

Role of the amino-terminal GAF domain of the NifA activator in controlling the response to the antiactivator protein NifL.

Molecular microbiology - 1 Jun 2004

Martinez-Argudo Isabel, Little Richard, Dixon Ray

Abstract excerpt

The NifA protein from Azotobacter vinelandii belongs to a family of enhancer binding proteins (EBPs) that activate transcription by RNA polymerase containing the sigma factor sigma(54). These proteins have conserved AAA+ domains that catalyse ATP hydrolysis to drive conformational changes necessary for open complex formation by sigma(54)-RNA polymerase. The activity of the NifA protein is highly regulated in...

Read the complete abstract on PubMed

Topics

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

Share to Azotobacter vinelandii
Share to beta-Galactosidase

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

Share to DNA-Directed RNA Polymerases

Share to Ketoglutaric Acids

Share to Nitrogen

Share to Nitrogen Fixation

Share to RNA Polymerase Sigma 54

Share to Sigma Factor

Source

Identifiers

PMID: 15186421
DOI: 10.1111/j.1365-2958.2004.04089.x

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.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Role of the amino-terminal GAF domain of the NifA activator in controlling the response to the antiactivator protein NifL.PMID 15186421Read ↗

Mutant forms of the Azotobacter vinelandii transcriptional activator NifA resistant to inhibition by the NifL regulatory protein.Semantic proximity Read ↗

Mutational analysis of the nucleotide-binding domain of the anti-activator NifL.Semantic proximity Read ↗

The product of the nitrogen fixation regulatory gene nfrX of Azotobacter vinelandii is functionally and structurally homologous to the uridylyltransferase encoded by glnD in enteric bacteria.Semantic proximity Read ↗

Role of Escherichia coli nitrogen regulatory genes in the nitrogen response of the Azotobacter vinelandii NifL-NifA complex.Semantic proximity Read ↗

Identification and functional characterization of NifA variants that are independent of GlnB activation in the photosynthetic bacterium Rhodospirillum rubrum.Semantic proximity Read ↗

Disrupting hierarchical control of nitrogen fixation enables carbon-dependent regulation of ammonia excretion in soil diazotrophs.Semantic proximity Read ↗

The role of regulatory genes nifA, vnfA, anfA, nfrX, ntrC, and rpoN in expression of genes encoding the three nitrogenases of Azotobacter vinelandii.Semantic proximity Read ↗

Competition between NarL-dependent activation and Fis-dependent repression controls expression from the Escherichia coli yeaR and ogt promoters.Semantic proximity Read ↗

Lethality of glnD null mutations in Azotobacter vinelandii is suppressible by prevention of glutamine synthetase adenylylation.Semantic proximity Read ↗

Functional roles for the GerE-family carboxyl-terminal domains of nitrate response regulators NarL and NarP of Escherichia coli K-12.Semantic proximity Read ↗

Peptidyl-prolyl cis/trans isomerase-independent functional NifH mutant of Azotobacter vinelandii.Semantic proximity Read ↗

Identification of a NifL-like protein in a diazotroph of the beta-subgroup of the Proteobacteria, Azoarcus sp. strain BH72.Semantic proximity Read ↗

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