ArticleJournal of bacteriology2003
Open reading frame sso2387 from the archaeon Sulfolobus solfataricus encodes a polypeptide with protein-serine kinase activity.
Article in Journal of bacteriology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 30 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
- 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
- Genome-wide identification and comprehensive analyses of the kinomes in four pathogenic microsporidia species.PloS one · 2014Article
- Archaeal signal transduction: impact of protein phosphatase deletions on cell size, motility, and energy metabolism in Sulfolobus acidocaldarius.Molecular & cellular proteomics : MCP · 2013Article
- Structure and function of the adhesive type IV pilus of Sulfolobus acidocaldarius.Environmental microbiology · 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
- Archaeal eukaryote-like serine/threonine protein kinase interacts with and phosphorylates a forkhead-associated-domain-containing protein.Journal of bacteriology · 2010Article
- Ser/Thr/Tyr protein phosphorylation in the archaeon Halobacterium salinarum--a representative of the third domain of life.PloS one · 2009Article
- 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
- A phosphoprotein from the archaeon Sulfolobus solfataricus with protein-serine/threonine kinase activity.Journal of bacteriology · 2004Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The predicted polypeptide product of open reading frame sso2387 from the archaeon Sulfolobus solfataricus, SsoPK2, displayed several of the sequence features conserved among the members of the "eukaryotic" protein kinase superfamily. sso2387 was cloned, and its polypeptide product was expressed in Escherichia coli. The recombinant protein, rSsoPK2, was recovered in insoluble aggregates that could be dispersed by using high concentrations (5 M) of urea. The solubilized polypeptide displayed the ability to phosphorylate itself as well as several exogenous proteins, including mixed histones, casein, bovine serum albumin, and reduced carboxyamidomethylated and maleylated lysozyme, on serine residues. The source of this activity resided in that portion of the protein displaying homology to the catalytic domain of eukaryotic protein kinases. By use of mass spectrometry, the sites of autophosphorylation were found to be located in two areas, one immediately N terminal to the region corresponding to subdomain I of eukaryotic protein kinases, and the second N terminal to the presumed activation loop located between subdomains VII and VIII. Autophosphorylation of rSsoPK2 could be uncoupled from the phosphorylation of exogenous proteins by manipulation of the temperature or mutagenic alteration of the enzyme. Autophosphorylation was detected only at temperatures >or=60 degrees C, whereas phosphorylation of exogenous proteins was detectable at 37 degrees C. Similarly, replacement of one of the potential sites of autophosphorylation, Ser(548), with alanine blocked autophosphorylation but not phosphorylation of an exogenous protein, casein.
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