ArticleProceedings of the National Academy of Sciences of the United States of America2001
A PP2C-type phosphatase dephosphorylates the PII signaling protein in the cyanobacterium Synechocystis PCC 6803.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed.
- PHLPP is neither a Phosphatase nor a Tumor Suppressor.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026Review
- The regulatory impact of serine/threonine-specific protein phosphorylation among cyanobacteria.Frontiers in plant science · 2025Review
- Mycobacterial serine/threonine phosphatase PstP is phosphoregulated and localized to mediate control of cell wall metabolism.Molecular microbiology · 2022Article
- Phosphorylation on PstP Regulates Cell Wall Metabolism and Antibiotic Tolerance in Mycobacterium smegmatis.Journal of bacteriology · 2021Article
- Carbon/nitrogen homeostasis control in cyanobacteria.FEMS microbiology reviews · 2020Review
- Inhibition of the Protein Phosphatase CppA Alters Development of Chlamydia trachomatis.Journal of bacteriology · 2018Article
- Phosphoproteome of the cyanobacterium Synechocystis sp. PCC 6803 and its dynamics during nitrogen starvation.Frontiers in microbiology · 2015Article
- Post-translational modification of P II signal transduction proteins.Frontiers in microbiology · 2014Review
- Review
- Structural and biochemical characterization of human mitochondrial branched-chain α-ketoacid dehydrogenase phosphatase.The Journal of biological chemistry · 2012Article
- A low molecular weight protein tyrosine phosphatase from Synechocystis sp. strain PCC 6803: enzymatic characterization and identification of its potential substrates.Journal of biochemistry · 2011Article
- Integrative analysis of large scale expression profiles reveals core transcriptional response and coordination between multiple cellular processes in a cyanobacterium.BMC systems biology · 2010Article
- Genomic structure of an economically important cyanobacterium, Arthrospira (Spirulina) platensis NIES-39.DNA research : an international journal for rapid publication of reports on genes and genomes · 2010Article
- Ecological genomics of marine picocyanobacteria.Microbiology and molecular biology reviews : MMBR · 2009Review
- Expression and mutational analysis of the glnB genomic region in the heterocyst-forming Cyanobacterium Anabaena sp. strain PCC 7120.Journal of bacteriology · 2009Article
- Identification of a novel PP2C-type mitochondrial phosphatase.Biochemical and biophysical research communications · 2007Article
- PII-regulated arginine synthesis controls accumulation of cyanophycin in Synechocystis sp. strain PCC 6803.Journal of bacteriology · 2006Article
- Identification of Rhodospirillum rubrum GlnB variants that are altered in their ability to interact with different targets in response to nitrogen status signals.Journal of bacteriology · 2006Article
- Signal transduction protein PII phosphatase PphA is required for light-dependent control of nitrate utilization in synechocystis sp. strain PCC 6803.Journal of bacteriology · 2005Article
- Diversity in domain architectures of Ser/Thr kinases and their homologues in prokaryotes.BMC genomics · 2005Article
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2 authors.
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No grant is acknowledged in the PubMed record.
Abstract
The family of the PII signal transduction proteins contains the most highly conserved signaling proteins in nature. The cyanobacterial PII-homologue transmits signals of the cellular nitrogen status and carbon status through phosphorylation of a seryl-residue. To identify the enzyme responsible for dephosphorylation of the phosphorylated PII protein in Synechocystis PCC 6803, prospective phosphatase encoding genes were inactivated by targeted insertion of kanamycin resistance cassettes. Disruption of ORF sll1771 generates a mutant unable to dephosphorylate PII under various experimental conditions. On the basis of conserved signature motifs, the sll1771 product (termed PphA) is a member of the protein phosphatase 2C (PP2C) superfamily, which is characterized by Mg(2+)/Mn(2+)-dependent catalytic activity. Biochemical analysis of overexpressed and purified PphA confirms its PP2C-type enzymatic properties and demonstrated its reactivity toward the phosphorylated PII protein. Thus, PphA is the first protein phosphatase in Synechocystis PCC 6803 for which the physiological substrate and function is known.
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