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 Phosphate Transport System Component PstB1 in Phosphate Internalization by Nostoc punctiforme.

Applied and environmental microbiology - 1 Nov 2016

Hudek L, Premachandra D, Webster W A J, Bräu L

Abstract excerpt

In bacteria, limited phosphate availability promotes the synthesis of active uptake systems, such as the Pst phosphate transport system. To understand the mechanisms that facilitate phosphate accumulation in the cyanobacterium Nostoc punctiforme, phosphate transport systems were identified, revealing a redundancy of Pst phosphate uptake systems that exists across three distinct operons. Four separate PstB system...

Read the complete abstract on PubMed

Topics

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

Share to Adenosine Triphosphatases
Share to ATP-Binding Cassette Transporters

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

Share to Bacterial Proteins

Share to Escherichia coli

Share to Gene Knockout Techniques

Share to Phosphates

Share to Real-Time Polymerase Chain Reaction

Share to RNA, Messenger

Source

Open in PubMed Open full text

Identifiers

PMID: 27542935
DOI: 10.1128/AEM.01336-16
PMCID: PMC5066351

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

Role of Phosphate Transport System Component PstB1 in Phosphate Internalization by Nostoc punctiforme.PMID 27542935Read ↗

Concurrent transcriptional activation of ppa and ppx genes by phosphate deprivation in the cyanobacterium Synechocystis sp. strain PCC 6803.Semantic proximity Read ↗

Molecular Mechanisms of Phosphate Sensing, Transport and Signalling in Streptomyces and Related ActinobacteriaSemantic proximity Read ↗

Regulon controlled by the GppX hybrid two component system in Porphyromonas gingivalis.Semantic proximity Read ↗

Characterization of a two-component signal transduction system involved in the induction of alkaline phosphatase under phosphate-limiting conditions in Synechocystis sp. PCC 6803.Semantic proximity Read ↗

Transcriptome analysis of Pantoea rara mutants reveals the underlying complexity of bacterial phosphate solubilization.Semantic proximity Read ↗

Genome-wide transcriptomic and proteomic analysis of the primary response to phosphate limitation in Streptomyces coelicolor M145 and in a DeltaphoP mutant.Semantic proximity Read ↗

Polyphosphate synthesis is essential for phosphate and ATP homeostasis during nutrient upshift.Semantic proximity Read ↗

Low-phosphate-selected Auxenochlorella protothecoides redirects phosphate to essential pathways while producing more biomass.Semantic proximity Read ↗

A novel non-catalytic function of PA2803-encoded PcrP contributes to polymyxin B resistance in P. aeruginosa and redefines the functional role of the PA2803 subfamily.Semantic proximity Read ↗

Identifying the suite of genes central to swimming in the biocontrol bacteria <i>Pseudomonas protegens</i> Pf-5Semantic proximity Read ↗

pbpB, a gene coding for a putative penicillin-binding protein, is required for aerobic nitrogen fixation in the cyanobacterium Anabaena sp. strain PCC7120.Semantic proximity Read ↗

Proteomic and phosphoproteomic analysis of a Haematococcus pluvialis (Chlorophyceae) mutant with a higher heterotrophic cell division rate reveals altered pathways involved in cell proliferation and nutrient partitioning.Semantic proximity Read ↗

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