ArticleJournal of bacteriology2004
Interactions between the nitrogen signal transduction protein PII and N-acetyl glutamate kinase in organisms that perform oxygenic photosynthesis.
Article in Journal of bacteriology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 48 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
48 citing papers in PubMed, 122 citations in OpenAlex.
- Amino Acids as Multifunctional Molecules in Plants: From Fundamental Metabolism to Precision Agriculture.Plants (Basel, Switzerland) · 2026Review
- Mutational analyses reveal PLP-independent functions at PipY, the cyanobacterial paradigm for pyridoxal-phosphate binding proteins.Scientific reports · 2026Article
- Article
- Structures of the cyanobacterial nitrogen regulators NtcA and PipX complexed to DNA shed light on DNA binding by NtcA and implicate PipX in the recruitment of RNA polymerase.Nucleic acids research · 2025Article
- Temperature changes are signaled in cyanobacteria through the PipX interaction network.Frontiers in microbiology · 2025Article
- Studies on the PII-PipX-NtcA Regulatory Axis of Cyanobacteria Provide Novel Insights into the Advantages and Limitations of Two-Hybrid Systems for Protein Interactions.International journal of molecular sciences · 2024Article
- Analysing the Cyanobacterial PipX Interaction Network Using NanoBiT Complementation inInternational journal of molecular sciences · 2024Article
- The Signal Transduction Protein PII Controls the Levels of the Cyanobacterial Protein PipX.Microorganisms · 2023Article
- The ribosome assembly GTPase EngA is involved in redox signaling in cyanobacteria.Frontiers in microbiology · 2023Article
- Pleiotropic effects of PipX, PipY, or RelQ overexpression on growth, cell size, photosynthesis, and polyphosphate accumulation in the cyanobacteriumFrontiers in microbiology · 2023Article
- The Conserved Family of the Pyridoxal Phosphate-Binding Protein (PLPBP) and Its Cyanobacterial Paradigm PipY.Life (Basel, Switzerland) · 2022Review
- The sRNA NsiR4 fine-tunes arginine synthesis in the cyanobacteriumRNA biology · 2022Article
- Reconstruction of the Diaminopimelic Acid Pathway to Promote L-lysine Production inInternational journal of molecular sciences · 2021Article
- Split NanoLuc technology allows quantitation of interactions between PII protein and its receptors with unprecedented sensitivity and reveals transient interactions.Scientific reports · 2021Article
- The Novel PmBio · 2021Article
- The novel PProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Regulatory Connections Between the Cyanobacterial Factor PipX and the Ribosome Assembly GTPase EngA.Frontiers in microbiology · 2021Article
- Distinctive Features of PipX, a Unique Signaling Protein of Cyanobacteria.Life (Basel, Switzerland) · 2020Review
- Carbon/nitrogen homeostasis control in cyanobacteria.FEMS microbiology reviews · 2020Review
- Enhancement of L-arginine production by increasing ammonium uptake in an AmtR-deficient Corynebacterium crenatum mutant.Journal of industrial microbiology & biotechnology · 2019Article
Corrections and comments
- Erratum issued
Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
PII, one of the most conserved signal transduction proteins, is believed to be a key player in the coordination of nitrogen assimilation and carbon metabolism in bacteria, archaea, and plants. However, the identity of PII receptors remains elusive, particularly in photosynthetic organisms. Here we used yeast two-hybrid approaches to identify new PII receptors and to explore the extent of conservation of PII signaling mechanisms between eubacteria and photosynthetic eukaryotes. Screening of Synechococcus sp. strain PCC 7942 libraries with PII as bait resulted in identification of N-acetyl glutamate kinase (NAGK), a key enzyme in the biosynthesis of arginine. The integrity of Ser49, a residue conserved in PII proteins from organisms that perform oxygenic photosynthesis, appears to be essential for NAGK binding. The effect of glnB mutations on NAGK activity is consistent with positive regulation of NAGK by PII. Phylogenetic and yeast two-hybrid analyses strongly suggest that there was conservation of the NAGK-PII regulatory interaction in the evolution of cyanobacteria and chloroplasts, providing insight into the function of eukaryotic PII-like proteins.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.