Protein polyphosphorylation of lysine residues by inorganic polyphosphate.

@article{Azevedo2015ProteinPO,
  title={Protein polyphosphorylation of lysine residues by inorganic polyphosphate.},
  author={Cristina Azevedo and Thomas Miles Livermore and Adolfo Saiardi},
  journal={Molecular cell},
  year={2015},
  volume={58 1},
  pages={71-82}
}
The complexity of higher organisms is not simply a reflection of the number of genes. A network of additional regulatory features, including protein post-translational modifications (PTMs), provides functional complexity otherwise inaccessible to a single gene product. Virtually all proteins are targets of PTMs. Here we characterize "polyphosphorylation" as the covalent attachment of inorganic polyphosphate (polyP) to target proteins. We found that nuclear signal recognition 1 (Nsr1) and its… CONTINUE READING
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Protein Polyphosphorylation of Lysine Residues by Inorganic Polyphosphate

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