Novel RNA-binding properties of Pop3p support a role for eukaryotic RNase P protein subunits in substrate recognition.

@article{Brusca2001NovelRP,
  title={Novel RNA-binding properties of Pop3p support a role for eukaryotic RNase P protein subunits in substrate recognition.},
  author={E M Brusca and Heather L True and Daniel W. Celander},
  journal={The Journal of biological chemistry},
  year={2001},
  volume={276 45},
  pages={
          42543-8
        }
}
Ribonuclease P (RNase P) catalyzes the 5'-end maturation of transfer RNA molecules. Recent evidence suggests that the eukaryotic protein subunits may provide substrate-binding functions (True, H. L., and Celander, D. W. (1998) J. Biol. Chem. 273, 7193-7196). We now report that Pop3p, an essential protein subunit of the holoenzyme in Saccharomyces cerevisiae, displays novel RNA-binding properties. A recombinant form of Pop3p (H6Pop3p) displays a 3-fold greater affinity for binding pre-tRNA… CONTINUE READING