ArticleJournal of bacteriology1999
The icfG gene cluster of Synechocystis sp. strain PCC 6803 encodes an Rsb/Spo-like protein kinase, protein phosphatase, and two phosphoproteins.
Article in Journal of bacteriology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 51 citations in OpenAlex.
- Inorganic carbon levels regulate growth via SigC signaling cascade in cyanobacteria.The New phytologist · 2025Article
- The RRM domain-containing protein Rbp3 interacts with ribosomes and the 3' ends of mRNAs encoding photosynthesis proteins.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- The regulatory impact of serine/threonine-specific protein phosphorylation among cyanobacteria.Frontiers in plant science · 2025Review
- Impact of nutrients on the function of the chlamydial Rsb partner switching mechanism.Pathogens and disease · 2022Article
- Integrative analysis of the salt stress response in cyanobacteria.Biology direct · 2021Article
- Post-translational Modifications of Serine/Threonine and Histidine Kinases and Their Roles in Signal Transductions in Synechocystis Sp. PCC 6803.Applied biochemistry and biotechnology · 2021Review
- Hanks-Type Serine/Threonine Protein Kinases and Phosphatases in Bacteria: Roles in Signaling and Adaptation to Various Environments.International journal of molecular sciences · 2018Review
- A transcriptional regulator Sll0794 regulates tolerance to biofuel ethanol in photosynthetic Synechocystis sp. PCC 6803.Molecular & cellular proteomics : MCP · 2014Article
- Post-translation modification in Archaea: lessons from Haloferax volcanii and other haloarchaea.FEMS microbiology reviews · 2013Review
- 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
- The protein phosphatases of Synechocystis sp. strain PCC 6803: open reading frames sll1033 and sll1387 encode enzymes that exhibit both protein-serine and protein-tyrosine phosphatase activity in vitro.Journal of bacteriology · 2005Article
- A phosphoprotein from the archaeon Sulfolobus solfataricus with protein-serine/threonine kinase activity.Journal of bacteriology · 2004Article
- Open reading frame sso2387 from the archaeon Sulfolobus solfataricus encodes a polypeptide with protein-serine kinase activity.Journal of bacteriology · 2003Article
- Phosphoprotein with phosphoglycerate mutase activity from the archaeon Sulfolobus solfataricus.Journal of bacteriology · 2003Article
- Archaeal protein kinases and protein phosphatases: insights from genomics and biochemistry.The Biochemical journal · 2003Review
- The membrane-associated protein-serine/threonine kinase from Sulfolobus solfataricus is a glycoprotein.Journal of bacteriology · 2002Article
- A PP2C-type phosphatase dephosphorylates the PII signaling protein in the cyanobacterium Synechocystis PCC 6803.Proceedings of the National Academy of Sciences of the United States of America · 2001Article
- The archaeon Sulfolobus solfataricus contains a membrane-associated protein kinase activity that preferentially phosphorylates threonine residues in vitro.Journal of bacteriology · 2000Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
A set of open reading frames (ORFs) potentially encoding signal transduction proteins are clustered around icfG, a gene implicated in the regulation of carbon metabolism, in the genome of Synechocystis sp. strain PCC 6803. slr1860 is the ORF for icfG, whose predicted product resembles the protein phosphatases SpoIIE, RsbU, and RsbX from Bacillus subtilis. Bracketing slr1860/icfG are (i) ORF slr1861, whose predicted product resembles the SpoIIAB, RsbT, and RsbW protein kinases from B. subtilis, and (ii) ORFs slr1856 and slr1859, whose predicted products resemble the respective phosphoprotein substrates for the B. subtilis protein kinases: SpoIIAA, RsbS, and RsbV. In order to determine whether the protein products encoded by these ORFs possessed the functional capabilities suggested by sequence comparisons, each was expressed in Escherichia coli as a histidine-tagged fusion protein and analyzed for its ability to participate in protein phosphorylation-dephosphorylation processes in vitro. It was observed that ORF slr1861 encoded an ATP-dependent protein kinase capable of phosphorylating Slr1856 and, albeit with noticeably lower efficiency, Slr1859. Site-directed mutagenesis suggests that Slr1861 phosphorylated these proteins on Ser-54 and Ser-57, respectively. Slr1860 exhibited divalent metal ion-dependent protein-serine phosphatase activity. It catalyzed the dephosphorylation of Slr1856, but not Slr1859, in vitro.
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