Evidence for auto-inhibition by the N terminus of hADAR2 and activation by dsRNA binding.

@article{MacBeth2004EvidenceFA,
  title={Evidence for auto-inhibition by the N terminus of hADAR2 and activation by dsRNA binding.},
  author={Mark MacBeth and Arunth T Lingam and Brenda L Bass},
  journal={RNA},
  year={2004},
  volume={10 10},
  pages={1563-71}
}
Adenosine deaminases that act on RNA (ADARs) catalyze adenosine to inosine conversion in RNA that is largely double stranded. Human ADAR2 (hADAR2) contains two double-stranded RNA binding motifs (dsRBMs), separated by a 90-amino acid linker, and these are followed by the C-terminal catalytic domain. We assayed enzymatic activity of N-terminal deletion constructs of hADAR2 to determine the role of the dsRBMs and the intervening linker peptide. We found that a truncated protein consisting of one… CONTINUE READING

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