Interactions of Exo1p with components of MutLalpha in Saccharomyces cerevisiae.

@article{Tran2001InteractionsOE,
  title={Interactions of Exo1p with components of MutLalpha in Saccharomyces cerevisiae.},
  author={Phuoc T. Tran and Julian A Simon and R. Michael Liskay},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2001},
  volume={98 17},
  pages={9760-5}
}
Previously, we reported evidence suggesting that Saccharomyces cerevisiae MutLalpha, composed of Mlh1p and Pms1p, was a functional member of the gyrase b/Hsp90/MutL (GHL) dimeric ATPase superfamily characterized by highly conserved ATPase domains. Similar to other GHL ATPases, these putative ATPase domains of MutLalpha may be important for the recruitment and/or activation of downstream effectors. One downstream effector candidate is Exo1p, a 5'-3' double stranded DNA exonuclease that has… CONTINUE READING

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