The DNA binding and oligomerization domain of MCM1 is sufficient for its interaction with other regulatory proteins.

@article{Primig1991TheDB,
  title={The DNA binding and oligomerization domain of MCM1 is sufficient for its interaction with other regulatory proteins.},
  author={Michael Primig and Herbert Winkler and Gustav Ammerer},
  journal={The EMBO journal},
  year={1991},
  volume={10 13},
  pages={
          4209-18
        }
}
The MCM1 gene encodes an essential DNA binding protein that, in cooperation with the transactivators alpha 1 and STE12 and the repressor alpha 2, confers mating specificity to haploid yeast cells. We show that the amino-terminal third of the MCM1 protein is sufficient for the physical interaction with these factors. A strain expressing just 98 amino acids encompassing the oligomerization and DNA binding domains of MCM1 is viable and mating competent. This motif exhibits considerable similarity… CONTINUE READING

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