ArticleJournal of bacteriology2000
The archaeon Sulfolobus solfataricus contains a membrane-associated protein kinase activity that preferentially phosphorylates threonine residues in vitro.
Article in Journal of bacteriology, 2000. 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
- Expanding the archaellum regulatory network - the eukaryotic protein kinases ArnC and ArnD influence motility of Sulfolobus acidocaldarius.MicrobiologyOpen · 2017Article
- Protein phosphorylation and its role in archaeal signal transduction.FEMS microbiology reviews · 2016Review
- 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
- Proteomic analysis of Sulfolobus solfataricus during Sulfolobus Turreted Icosahedral Virus infection.Journal of proteome research · 2012Article
- Identification and characterization of a leucine-rich repeat kinase 2 (LRRK2) consensus phosphorylation motif.PloS one · 2010Article
- Plasmids and viruses of the thermoacidophilic crenarchaeote Sulfolobus.Extremophiles : life under extreme conditions · 2006Review
- Posttranslational protein modification in Archaea.Microbiology and molecular biology reviews : MMBR · 2005Review
- 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
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Authors and funding
3 authors at 1 institution in 1 country.
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Abstract
The extreme acidothermophilic archaeon Sulfolobus solfataricus harbors a membrane-associated protein kinase activity. Its solubilization and stabilization required detergents, suggesting that this activity resides within an integral membrane protein. The archaeal protein kinase utilized purine nucleotides as phosphoryl donors in vitro. A noticeable preference for nucleotide triphosphates over nucleotide diphosphates and for adenyl nucleotides over the corresponding guanyl ones was observed. The molecular mass of the solubilized, partially purified enzyme was estimated to be approximately 125 kDa by gel filtration chromatography. Catalytic activity resided in a polypeptide with an apparent molecular mass of approximately 67 kDa by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Challenges with several exogenous substrates revealed the protein kinase to be relatively selective. Only casein, histone H4, reduced carboxyamidomethylated and maleylated lysozyme, and a peptide modeled after myosin light chains (KKRAARATSNVFA) were phosphorylated to appreciable levels in vitro. All of the aforementioned substrates were phosphorylated on threonine residues, while histone H4 was phosphorylated on serine as well. Substitution of serine for the phosphoacceptor threonine in the myosin light chain peptide produced a noticeably inferior substrate. The protein kinase underwent autophosphorylation on threonine and was relatively insensitive to a set of known inhibitors of "eukaryotic" protein kinases.
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