Production of "authentic" poliovirus RNA-dependent RNA polymerase (3D(pol)) by ubiquitin-protease-mediated cleavage in Escherichia coli.

@article{Gohara1999ProductionO,
  title={Production of "authentic" poliovirus RNA-dependent RNA polymerase (3D(pol)) by ubiquitin-protease-mediated cleavage in Escherichia coli.},
  author={David Gohara and Chang Su Ha and Sundramurthy Kumar and Brahma Ghosh and Jamie J Arnold and Timothy Wisniewski and Craig E Cameron},
  journal={Protein expression and purification},
  year={1999},
  volume={17 1},
  pages={
          128-38
        }
}
The first amino acid of "authentic" poliovirus RNA-dependent RNA polymerase, 3D(pol), is a glycine. As a result, production of 3D(pol) in Escherichia coli requires addition of an initiation codon; thus, a formylmethionine is added to the amino terminus. The formylmethionine should be removed by the combined action of a cellular deformylase and methionine aminopeptidase. However, high-level expression of 3D(pol) in E. coli yields enzyme with a heterogeneous amino terminus. To preclude this… CONTINUE READING
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