Learn More
Budding yeast HAP2 is required in concert with HAP3 and HAP4 to form a heterotrimeric CCAAT-binding transcriptional activation complex at the UAS2 element of CYC1. Functional homologs of HAP2 and HAP3 have been conserved in HeLa cells where HAP2 activity corresponds to a chromatographic fraction designated CP1B. Here, we describe deletion and codon(More)
The S. cerevisiae HAP2 and HAP3 gene products have been shown to recognize CCAAT-containing transcription elements as a HAP2/HAP3 multisubunit heterologous complex, or heteromer. Recently, we have demonstrated that the human sequence-specific DNA-binding protein, CP1, also recognizes CCAAT-containing transcription elements as a heteromer. Mammalian cells(More)
Activation of the CYC1 upstream activation site (UAS2) and other Saccharomyces cerevisiae genes encoding respiratory functions requires the products of the regulatory loci HAP2 and HAP3. We present here the DNA sequence of the yeast HAP2 gene and an initial investigation into the function of its product. The DNA sequence indicated that HAP2 encoded a(More)
BACKGROUND AND PURPOSE It is unclear whether delayed-type hypersensitivity reactions against implanted metals play a role in the etiopathogenesis of malfunctioning total knee arthroplasties. We therefore evaluated the association between metal allergy, defined as a positive patch test reaction to common metal allergens, and revision surgery in patients who(More)
Open Access-This article is distributed under the terms of the Creative Commons Attribution Noncommercial License which permits any noncommercial use, distribution, and reproduction in any medium, provided the source is credited. Background and purpose — It is unclear whether delayed-type hypersensitivity reactions against implanted metals play a role in(More)
Transcriptional activation by the yeast CYC1 upstream activation site UAS2UP1 requires the products of both the HAP2 and HAP3 regulatory genes. We show here that both HAP2 and HAP3 in yeast extracts bind to UAS2UP1 and give rise to a single protein-DNA complex, termed C, in nondenaturing polyacrylamide gels. That both products are a part of complex C was(More)
The fission yeast Schizosaccharomyces pombe is immensely diverged from budding yeast (Saccharomyces cerevisiae) on an evolutionary time scale. We have used a fission yeast library to clone a homolog of S. cerevisiae HAP2, which along with HAP3 and HAP4 forms a transcriptional activation complex that binds to the CCAAT box. The S. pombe homolog php2 (S.(More)
We dissected the domain of HAP2 that mediates subunit association in the heteromeric CCAAT-binding complex, first by genetic mutational analysis and then by structural studies. The mutational data suggest that a very short region in HAP2 mediates protein-protein association and that the structure of this domain is likely to be an alpha-helix. The CD(More)
  • 1