Interaction of Escherichia coli DbpA with 23S rRNA in different functional states of the enzyme.

@article{Karginov2004InteractionOE,
  title={Interaction of Escherichia coli DbpA with 23S rRNA in different functional states of the enzyme.},
  author={Fedor V. Karginov and O. C. Uhlenbeck},
  journal={Nucleic acids research},
  year={2004},
  volume={32 10},
  pages={3028-32}
}
DEx(D)/(H) proteins catalyze structural rearrangements in RNA by coupling ATP hydrolysis to the destabilization of RNA helices or RNP complexes. The Escherichia coli DEx(D)/(H) protein DbpA specifically recognizes a region within the catalytic core of 23S rRNA. To better characterize the interaction of DbpA with this region and to identify changes in the complex between different nucleotide-bound states of the enzyme, RNase T1, RNase T2, kethoxal and DMS footprinting of DbpA on a 172 nt… CONTINUE READING

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