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Functional dissection and sequence of yeast HAP1 activator.

K Pfeifer1, K S Kim, S Kogan

  • 1Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.

Cell
|January 27, 1989
PubMed
Summary
This summary is machine-generated.

Researchers dissected the yeast activator HAP1, identifying a DNA binding domain with a zinc finger crucial for target site recognition. A separate region mediates heme induction, while the carboxyl terminus drives transcriptional activation.

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Area of Science:

  • Molecular Biology
  • Yeast Genetics
  • Transcription Factors

Background:

  • The yeast activator HAP1 is a key regulator of gene expression.
  • Understanding its DNA binding and regulatory mechanisms is crucial for deciphering cellular processes.

Purpose of the Study:

  • To functionally dissect the 1483-residue yeast activator HAP1.
  • To identify specific domains responsible for DNA binding, heme induction, and transcriptional activation.

Main Methods:

  • Site-directed mutagenesis to alter specific residues within HAP1.
  • DNA binding assays to assess HAP1's interaction with target sites (UAS1 and CYC7).
  • Analysis of HAP1's functional domains through mutational studies.

Main Results:

  • A single DNA binding domain (residues 1-148) containing a cysteine-rich zinc finger mediates binding to UAS1 and CYC7.
  • Specific mutations within or flanking the zinc finger abolish binding to UAS1 or CYC7, indicating sequence-specific recognition.
  • A distinct region (residues 245-445) is involved in heme induction by masking the DNA binding domain, with heme counteracting this effect.
  • A highly acidic carboxyl terminus is essential for HAP1-mediated transcriptional activation.

Conclusions:

  • HAP1's DNA binding specificity is determined by its zinc finger and adjacent residues.
  • Heme induction involves a masking mechanism regulated by a metal-binding repeat region.
  • The carboxyl terminus acts as the primary transcriptional activation domain of HAP1.