Probing the mechanisms of DEAD-box proteins as general RNA chaperones: the C-terminal domain of CYT-19 mediates general recognition of RNA.

@article{Grohman2007ProbingTM,
  title={Probing the mechanisms of DEAD-box proteins as general RNA chaperones: the C-terminal domain of CYT-19 mediates general recognition of RNA.},
  author={Jacob K Grohman and Mark Del Campo and Hari Bhaskaran and Pilar Tijerina and Alan M. Lambowitz and Rick Russell},
  journal={Biochemistry},
  year={2007},
  volume={46 11},
  pages={3013-22}
}
The DEAD-box protein CYT-19 functions in the folding of several group I introns in vivo and a diverse set of group I and group II RNAs in vitro. Recent work using the Tetrahymena group I ribozyme demonstrated that CYT-19 possesses a second RNA-binding site, distinct from the unwinding active site, which enhances unwinding activity by binding nonspecifically to the adjacent RNA structure. Here, we probe the region of CYT-19 responsible for that binding by constructing a C-terminal truncation… CONTINUE READING

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