ArticleThe Journal of biological chemistry2014
Structural basis and target-specific modulation of ADP sensing by the Synechococcus elongatus PII signaling protein.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 69 citations in OpenAlex.
- Ability ofMicroorganisms · 2026Article
- Calcium-induced PII oligomerization enhances physiological performance in the cyanobacterium Synechococcus elongatus PCC 7942.Archives of microbiology · 2026Article
- 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
- In Vivo Detection of Metabolic Fluctuations in Real Time Using the NanoBiT Technology Based on PII Signalling Protein Interactions.International journal of molecular sciences · 2024Article
- Allosteric regulation of nitrate transporter NRT via the signaling protein PII.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- The Signal Transduction Protein PII Controls the Levels of the Cyanobacterial Protein PipX.Microorganisms · 2023Article
- Pleiotropic effects of PipX, PipY, or RelQ overexpression on growth, cell size, photosynthesis, and polyphosphate accumulation in the cyanobacteriumFrontiers in microbiology · 2023Article
- The ribosome assembly GTPase EngA is involved in redox signaling in cyanobacteria.Frontiers in microbiology · 2023Article
- The Conserved Family of the Pyridoxal Phosphate-Binding Protein (PLPBP) and Its Cyanobacterial Paradigm PipY.Life (Basel, Switzerland) · 2022Review
- Arginine inhibition of the argininosuccinate lyases is conserved among three orders in cyanobacteria.Plant molecular biology · 2022Article
- 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
- NADThe Journal of biological chemistry · 2020Article
- Carbon/nitrogen homeostasis control in cyanobacteria.FEMS microbiology reviews · 2020Review
- Tuning the in vitro sensing and signaling properties of cyanobacterial PII protein by mutation of key residues.Scientific reports · 2019Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
PII signaling proteins comprise one of the most versatile signaling devices in nature and have a highly conserved structure. In cyanobacteria, PipX and N-acetyl-L-glutamate kinase are receptors of PII signaling, and these interactions are modulated by ADP, ATP, and 2-oxoglutarate. These effector molecules bind interdependently to three anti-cooperative binding sites on the trimeric PII protein and thereby affect its structure. Here we used the PII protein from Synechococcus elongatus PCC 7942 to reveal the structural basis of anti-cooperative ADP binding. Furthermore, we clarified the mutual influence of PII-receptor interaction and sensing of the ATP/ADP ratio. The crystal structures of two forms of trimeric PII, one with one ADP bound and the other with all three ADP-binding sites occupied, revealed significant differences in the ADP binding mode: at one site (S1) ADP is tightly bound through side-chain and main-chain interactions, whereas at the other two sites (S2 and S3) the ADP molecules are only bound by main-chain interactions. In the presence of the PII-receptor PipX, the affinity of ADP to the first binding site S1 strongly increases, whereas the affinity for ATP decreases due to PipX favoring the S1 conformation of PII-ADP. In consequence, the PII-PipX interaction is highly sensitive to subtle fluctuations in the ATP/ADP ratio. By contrast, the PII-N-acetyl-L-glutamate kinase interaction, which is negatively affected by ADP, is insensitive to these fluctuations. Modulation of the metabolite-sensing properties of PII by its receptors allows PII to differentially perceive signals in a target-specific manner and to perform multitasking signal transduction.
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