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

A role for the signal transduction protein PII in the control of nitrate/nitrite uptake in a cyanobacterium.

FEBS letters - 8 May 1998

Lee H M, Flores E, Herrero A, Houmard J, Tandeau de Marsac N

Abstract excerpt

In the cyanobacterium Synechococcus sp. strain PCC 7942, ammonium exerts a rapid and reversible inhibition of the nitrate and nitrite uptake, and the PII protein (GlnB) is differentially phosphorylated depending on the intracellular N/C balance. RNA/DNA hybridizations, as well as nitrate and nitrite uptake experiments, were carried out with the wild-type strain and a PII-null mutant. The transcriptional control...

Read the complete abstract on PubMed

Topics

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

Share to Bacterial Proteins
Share to Cyanobacteria
Share to Mutation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Operon

Share to Phosphorylation

Share to RNA, Bacterial

Share to RNA, Messenger

Share to Signal Transduction

Source

Identifiers

PMID: 9607331
DOI: 10.1016/s0014-5793(98)00451-7

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

A role for the signal transduction protein PII in the control of nitrate/nitrite uptake in a cyanobacterium.PMID 9607331Read ↗

Phosphorylation of the signal transducer PII protein and an additional effector are required for the PII-mediated regulation of nitrate and nitrite uptake in the Cyanobacterium synechococcus sp. PCC 7942.Semantic proximity Read ↗

Functional analysis of the phosphoprotein PII (glnB gene product) in the cyanobacterium Synechococcus sp. strain PCC 7942.Semantic proximity Read ↗

Transcriptional effects of the signal transduction protein P(II) (glnB gene product) on NtcA-dependent genes in Synechococcus sp. PCC 7942.Semantic proximity Read ↗

The global nitrogen regulator NtcA regulates transcription of the signal transducer PII (GlnB) and influences its phosphorylation level in response to nitrogen and carbon supplies in the Cyanobacterium synechococcus sp. strain PCC 7942.Semantic proximity Read ↗

Effects of PII deficiency on expression of the genes involved in ammonium utilization in the cyanobacterium Synechocystis sp. Strain PCC 6803.Semantic proximity Read ↗

Cell-type specific modification of PII is involved in the regulation of nitrogen metabolism in the cyanobacterium Anabaena PCC 7120.Semantic proximity Read ↗

Cloning and characterisation of the pknD gene encoding an eukaryotic-type protein kinase in the cyanobacterium Anabaena sp. PCC7120.Semantic proximity Read ↗

Signal transduction protein PII phosphatase PphA is required for light-dependent control of nitrate utilization in synechocystis sp. strain PCC 6803.Semantic proximity Read ↗

Protein phosphatase PphA from Synechocystis sp. PCC 6803: the physiological framework of PII-P dephosphorylation.Semantic proximity Read ↗

Identification of PamA as a PII-binding membrane protein important in nitrogen-related and sugar-catabolic gene expression in Synechocystis sp. PCC 6803.Semantic proximity Read ↗

PII is important in regulation of nitrogen metabolism but not required for heterocyst formation in the Cyanobacterium Anabaena sp. PCC 7120.Semantic proximity Read ↗

Dissection of the Mechanisms of Growth Inhibition Resulting from Loss of the PII Protein in the Cyanobacterium Synechococcus elongatus PCC 7942.Semantic proximity Read ↗

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