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

Mutations affecting motifs of unknown function in the central domain of nitrogen regulatory protein C.

Journal of bacteriology - 1 Sept 1999

Li J, Passaglia L, Rombel I, Yan D, Kustu S

Abstract excerpt

The positive control function of the bacterial enhancer-binding protein NtrC resides in its central domain, which is highly conserved among activators of sigma54 holoenzyme. Previous studies of a small set of mutant forms specifically defective in transcriptional activation, called NtrC repressor [NtrC(Rep)] proteins, had enabled us to locate various functional determinants in the central domain. In this more...

Read the complete abstract on PubMed

Topics

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

Share to Chromosomes, Bacterial
Share to Glutamate-Ammonia Ligase
Share to Holoenzymes

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

Share to Lac Operon

Share to PII Nitrogen Regulatory Proteins

Share to RNA Polymerase Sigma 54

Share to Sigma Factor

Share to Solubility

Source

Open in PubMed Open full text

Identifiers

PMID: 10464219
DOI: 10.1128/JB.181.17.5443-5454.1999
PMCID: PMC94054

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

Mutations affecting motifs of unknown function in the central domain of nitrogen regulatory protein C.PMID 10464219Read ↗

Phosphorylation-independent dimer-dimer interactions by the enhancer-binding activator NtrC of Escherichia coli: a third function for the C-terminal domain.Semantic proximity Read ↗

Constitutive forms of the enhancer-binding protein NtrC: evidence that essential oligomerization determinants lie in the central activation domain.Semantic proximity Read ↗

The major dimerization determinants of the nitrogen regulatory protein NTRC from enteric bacteria lie in its carboxy-terminal domain.Semantic proximity Read ↗

The function of isolated domains and chimaeric proteins constructed from the transcriptional activators NifA and NtrC of Klebsiella pneumoniae.Semantic proximity Read ↗

Crystal structure of the C-terminal domain of the two-component system transmitter protein nitrogen regulator II (NRII; NtrB), regulator of nitrogen assimilation in Escherichia coli.Semantic proximity Read ↗

NtcA, a global nitrogen regulator from the cyanobacterium Synechococcus that belongs to the Crp family of bacterial regulators.Semantic proximity Read ↗

Alterations of highly conserved residues in the regulatory domain of nitrogen regulator I (NtrC) of Escherichia coli.Semantic proximity Read ↗

Amino acid residues critical for DNA binding and inducer recognition in CbnR, a LysR-type transcriptional regulator from Cupriavidus necator NH9.Semantic proximity Read ↗

The CnuK9E H-NS complex antagonizes DNA binding of DicA and leads to temperature-dependent filamentous growth in E. coli.Semantic proximity Read ↗

Mapping the phenotypic landscape of a transcriptional repressor using deep mutational scanning and growth-based quantitative sequencing.Semantic proximity Read ↗

Mutations altering the N-terminal receiver domain of NRI (NtrC) That prevent dephosphorylation by the NRII-PII complex in Escherichia coli.Semantic proximity Read ↗

Cnu, a novel oriC-binding protein of Escherichia coli.Semantic proximity Read ↗

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