The domain order of mammalian capping enzyme can be inverted and baculovirus phosphatase can function in cap formation in vivo.

@article{Martins2002TheDO,
  title={The domain order of mammalian capping enzyme can be inverted and baculovirus phosphatase can function in cap formation in vivo.},
  author={A. Martins and S. Shuman},
  journal={Virology},
  year={2002},
  volume={304 2},
  pages={
          167-75
        }
}
  • A. Martins, S. Shuman
  • Published 2002
  • Biology, Medicine
  • Virology
  • The bifunctional mammalian mRNA capping enzyme (Mce1) consists of an N-terminal triphosphatase domain Mce1(1-210) fused to a C-terminal guanylyltransferase domain Mce1(211-597). The physical domain order H(2)N-triphosphatase-guanylyltransferase-COOH mimics the temporal order of the capping reactions. To determine if the physical domain order is functionally important in vivo, we engineered an "inverted" mammalian capping enzyme InvMce1 [H(2)N-Mce1(211-597)-(1-210)-COOH]. We found that InvMce1… CONTINUE READING
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