Characterization of bacteriophage KVP40 and T4 RNA ligase 2.

@article{Yin2004CharacterizationOB,
  title={Characterization of bacteriophage KVP40 and T4 RNA ligase 2.},
  author={Shenmin Yin and C Kiong Ho and Eric S. Miller and Stewart Shuman},
  journal={Virology},
  year={2004},
  volume={319 1},
  pages={141-51}
}
Bacteriophage T4 RNA ligase 2 (Rnl2) exemplifies a subfamily of RNA strand-joining enzymes that includes the trypanosome RNA editing ligases. A homolog of T4 Rnl2 is encoded in the 244-kbp DNA genome of vibriophage KVP40. We show that the 335-amino acid KVP40 Rnl2 is a monomeric protein that catalyzes RNA end-joining through ligase-adenylate and RNA-adenylate (AppRNA) intermediates. In the absence of ATP, pre-adenylated KVP40 Rnl2 reacts with an 18-mer 5'-PO(4) single-strand RNA (pRNA) to form… CONTINUE READING

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