Effect of mutations in a zinc-binding domain of yeast RNA polymerase C (III) on enzyme function and subunit association.

@article{Werner1992EffectOM,
  title={Effect of mutations in a zinc-binding domain of yeast RNA polymerase C (III) on enzyme function and subunit association.},
  author={Michel Werner and Sylvie Hermann-Le Denmat and I Treich and A. Sentenac and Pierre Thuriaux},
  journal={Molecular and cellular biology},
  year={1992},
  volume={12 3},
  pages={1087-95}
}
The conserved amino-terminal region of the largest subunit of yeast RNA polymerase C is capable of binding zinc ions in vitro. By oligonucleotide-directed mutagenesis, we show that the putative zinc-binding motif CX2CX6-12CXGHXGX24-37CX2C, present in the largest subunit of all eukaryotic and archaebacterial RNA polymerases, is essential for the function of RNA polymerase C. All mutations in the invariant cysteine and histidine residues conferred a lethal phenotype. We also obtained two… CONTINUE READING

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