ArticleJournal of bacteriology2004
A phosphoprotein from the archaeon Sulfolobus solfataricus with protein-serine/threonine kinase activity.
Article in Journal of bacteriology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 25 citations in OpenAlex.
- The biology of thermoacidophilic archaea from the order Sulfolobales.FEMS microbiology reviews · 2021Article
- Novel Tyrosine Kinase-Mediated Phosphorylation With Dual Specificity Plays a Key Role in the Modulation ofFrontiers in microbiology · 2021Article
- Expanding the archaellum regulatory network - the eukaryotic protein kinases ArnC and ArnD influence motility of Sulfolobus acidocaldarius.MicrobiologyOpen · 2017Article
- Autophosphorylation and Cross-Phosphorylation of Protein Kinases from the CrenarchaeonFrontiers in microbiology · 2017Article
- Protein phosphorylation and its role in archaeal signal transduction.FEMS microbiology reviews · 2016Review
- Article
- Protein Ser/Thr/Tyr phosphorylation in the Archaea.The Journal of biological chemistry · 2014Review
- Carbohydrate metabolism in Archaea: current insights into unusual enzymes and pathways and their regulation.Microbiology and molecular biology reviews : MMBR · 2014Review
- Archaeal signal transduction: impact of protein phosphatase deletions on cell size, motility, and energy metabolism in Sulfolobus acidocaldarius.Molecular & cellular proteomics : MCP · 2013Article
- Article
- Archaeal eukaryote-like serine/threonine protein kinase interacts with and phosphorylates a forkhead-associated-domain-containing protein.Journal of bacteriology · 2010Article
- Article
- Posttranslational protein modification in Archaea.Microbiology and molecular biology reviews : MMBR · 2005Review
- A phosphohexomutase from the archaeon Sulfolobus solfataricus is covalently modified by phosphorylation on serine.Journal of bacteriology · 2005Article
- Identification and characterization of Sulfolobus solfataricus D-gluconate dehydratase: a key enzyme in the non-phosphorylated Entner-Doudoroff pathway.The Biochemical journal · 2005Article
Corrections and comments
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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
Sulfolobus solfataricus contains a membrane-associated protein kinase activity that displays a strong preference for threonine as the phospho-acceptor amino acid residue. When a partially purified detergent extract of the membrane fraction from the archaeon S. solfataricus that had been enriched for this activity was incubated with [gamma-(32)P]ATP, radiolabeled phosphate was incorporated into roughly a dozen polypeptides, several of which contained phosphothreonine. One of the phosphothreonine-containing proteins was identified by mass peptide profiling as the product of open reading frame [ORF] sso0469. Inspection of the DNA-derived amino acid sequence of the predicted protein product of ORF sso0469 revealed the presence of sequence characteristics faintly reminiscent of the "eukaryotic" protein kinase superfamily. ORF sso0469 therefore was cloned, and its polypeptide product was expressed in Escherichia coli. The recombinant protein formed insoluble aggregates that could be dispersed using urea or detergents. The solubilized polypeptide phosphorylated several exogenous proteins in vitro, including casein, myelin basic protein, and bovine serum albumin. Mutagenic alteration of amino acids predicted to be essential for catalytic activity abolished or severely reduced catalytic activity. Phosphorylation of exogenous substrates took place on serine and, occasionally, threonine. This new archaeal protein kinase displayed no catalytic activity when GTP was substituted for ATP as the phospho-donor substrate, while Mn(2+) was the preferred cofactor.
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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.