Global phosphoproteomic analysis reveals diverse functions of serine/threonine/tyrosine phosphorylation in the model cyanobacterium Synechococcus sp. strain PCC 7002.

@article{Yang2013GlobalPA,
  title={Global phosphoproteomic analysis reveals diverse functions of serine/threonine/tyrosine phosphorylation in the model cyanobacterium Synechococcus sp. strain PCC 7002.},
  author={Ming-kun Yang and Zhi-Xian Qiao and Wan-yi Zhang and Qian Xiong and Jia Zhang and Tao Li and Feng Ge and Jin-dong Zhao},
  journal={Journal of proteome research},
  year={2013},
  volume={12 4},
  pages={1909-23}
}
Increasing evidence shows that protein phosphorylation on serine (Ser), threonine (Thr), and tyrosine (Tyr) residues is one of the major post-translational modifications in the bacteria, involved in regulating a myriad of physiological processes. Cyanobacteria are one of the largest groups of bacteria and are the only prokaryotes capable of oxygenic photosynthesis. Many cyanobacteria strains contain unusually high numbers of protein kinases and phosphatases with specificity on Ser, Thr, and Tyr… CONTINUE READING
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