Transphosphorylation of E-coli Proteins and Kinase Specificity
Reporter: Larry H Bernstein, MD, FCAP
https://pharmaceuticalintelligence.com/2013/03/04/transphosphory…i-ptoteins-and/
X Wu, Man-Ho Oh, HS Kim, D Schwartz,… Huber SC.
Front. Plant Sci. 3:262. http://dx.doi.org/ 10.3389/fpls.2012.00262
Four lines of evidence suggest that transphosphorylation of E. coli proteins by BRI1
is specific and therefore provides meaningful results:
(1) phosphorylation is
- not correlated with bacterial protein abundance;
(2) phosphosite stoichiometry, estimated by spectral counting, is also
- not related to protein abundance;
(3) a transphosphorylation motif emerged
- with strong preference for basic residues both N- and C-terminal to the phosphosites; and
(4) other protein kinases (BAK1, PEPR1, FLS2, and CDPKβ) phosphorylated a distinct set of E. coli proteins and phosphosites. http://fpls.com/Transphosphorylation_of_E._coli_proteins_during_production_of_recombinant_protein_kinases_provides_a_robust_system_to_characterize_kinase_specificity/
English: Structure of the BAK1 protein. Based on PyMOL rendering of PDB 2ims. (Photo credit: Wikipedia)
Escherichia coli – Scanning Electron Microscopy (Photo credit: Wikipedia)
English: Protein kinase CK2, a phosphorylation enzyme (Photo credit: Wikipedia)
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*Transphosphorylation *
also important for PTM
On Thu, Jul 24, 2014 at 1:29 PM, Pharmaceutical Intelligence wrote:
>