The archaeon Sulfolobus solfataricus contains a membrane-associated protein kinase activity that preferentially phosphorylates threonine residues in vitro.

@article{Lower2000TheAS,
  title={The archaeon Sulfolobus solfataricus contains a membrane-associated protein kinase activity that preferentially phosphorylates threonine residues in vitro.},
  author={Brian Howard Lower and Kenneth M Bischoff and Peter J. Kennelly},
  journal={Journal of bacteriology},
  year={2000},
  volume={182 12},
  pages={
          3452-9
        }
}
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… CONTINUE READING

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References

Publications referenced by this paper.
SHOWING 1-10 OF 44 REFERENCES

Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3.

  • DNA research : an international journal for rapid publication of reports on genes and genomes
  • 1998
VIEW 1 EXCERPT

New protein kinase and protein phosphatase families mediate signal transduction in bacterial catabolite repression.

  • Proceedings of the National Academy of Sciences of the United States of America
  • 1998
VIEW 1 EXCERPT