Phosphorylation of the PII protein (glnB gene product) in the cyanobacterium Synechococcus sp. strain PCC 7942: analysis of in vitro kinase activity.

@article{Forchhammer1995PhosphorylationOT,
  title={Phosphorylation of the PII protein (glnB gene product) in the cyanobacterium Synechococcus sp. strain PCC 7942: analysis of in vitro kinase activity.},
  author={Karl Forchhammer and Nicole Tandeau de Marsac},
  journal={Journal of bacteriology},
  year={1995},
  volume={177 20},
  pages={5812-7}
}
The PII protein in the cyanobacterium Synechococcus sp. strain PCC 7942 signals the cellular state of nitrogen assimilation relative to CO2 fixation by being phosphorylated at a seryl residue. In this study, we first determined the location of the phosphorylated seryl residue within the PII amino acid sequence. The phosphorylation site exhibits an RXS motif, a recognition sequence characteristic for cyclic AMP-dependent protein serine kinases from eukaryotes. We established an in vitro PII… CONTINUE READING

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