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Article

Interaction network in cyanobacterial nitrogen regulation: PipX, a protein that interacts in a 2-oxoglutarate dependent manner with PII and NtcA.

Molecular microbiology - 1 Jul 2006

Espinosa Javier, Forchhammer Karl, Burillo Sergio, Contreras Asunción

Abstract excerpt

Cyanobacteria perceive nitrogen status by sensing intracellular 2-oxoglutarate levels. The global nitrogen transcription factor NtcA and the signal transduction protein PII are both involved in 2-oxoglutarate sensing. PII proteins, probably the most conserved signal transduction proteins in nature, are remarkable for their ability to interact with very diverse protein targets in different systems. Despite...

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PMID: 16796668
DOI: 10.1111/j.1365-2958.2006.05231.x

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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.

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Interaction network in cyanobacterial nitrogen regulation: PipX, a protein that interacts in a 2-oxoglutarate dependent manner with PII and NtcA.PMID 16796668Read ↗

PipX, the coactivator of NtcA, is a global regulator in cyanobacteria.Semantic proximity Read ↗

Structural basis for the regulation of NtcA-dependent transcription by proteins PipX and PII.Semantic proximity Read ↗

P(II) signal transduction proteins are ATPases whose activity is regulated by 2-oxoglutarate.Semantic proximity Read ↗

Mutations at pipX suppress lethality of PII-deficient mutants of Synechococcus elongatus PCC 7942.Semantic proximity Read ↗

Specific role of the cyanobacterial PipX factor in the heterocysts of Anabaena sp. strain PCC 7120.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 ↗

Regulation of autophosphorylation of Escherichia coli nitrogen regulator II by the PII signal transduction protein.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 ↗

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 ↗

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

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

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