Mutational and structural analyses of the ribonucleotide reductase inhibitor Sml1 define its Rnr1 interaction domain whose inactivation allows suppression of mec1 and rad53 lethality.

@article{Zhao2000MutationalAS,
  title={Mutational and structural analyses of the ribonucleotide reductase inhibitor Sml1 define its Rnr1 interaction domain whose inactivation allows suppression of mec1 and rad53 lethality.},
  author={Xin Zhao and Bilyana Georgieva and Andrei Chabes and Vladimir Domkin and Johannes H. Ippel and J{\"u}rgen Schleucher and Sybren Wijmenga and Lars Thelander and Rodney Rothstein},
  journal={Molecular and cellular biology},
  year={2000},
  volume={20 23},
  pages={9076-83}
}
In budding yeast, MEC1 and RAD53 are essential for cell growth. Previously we reported that mec1 or rad53 lethality is suppressed by removal of Sml1, a protein that binds to the large subunit of ribonucleotide reductase (Rnr1) and inhibits RNR activity. To understand further the relationship between this suppression and the Sml1-Rnr1 interaction, we randomly mutagenized the SML1 open reading frame. Seven mutations were identified that did not affect protein expression levels but relieved mec1… CONTINUE READING

Citations

Publications citing this paper.
Showing 1-10 of 38 extracted citations

Similar Papers

Loading similar papers…