The Schizosaccharomyces pombe homolog of Saccharomyces cerevisiae HAP2 reveals selective and stringent conservation of the small essential core protein domain
Autor: | J D Fikes, J T Olesen, Leonard Guarente |
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Jazyk: | angličtina |
Rok vydání: | 1991 |
Předmět: |
Protein subunit
Mutant Saccharomyces cerevisiae Molecular Sequence Data Restriction Mapping CAAT box Fungal Proteins Sequence Homology Nucleic Acid Schizosaccharomyces Amino Acid Sequence Cloning Molecular Molecular Biology Gene Library Genetics Fungal protein biology Base Sequence Genetic Complementation Test Cell Biology biology.organism_classification beta-Galactosidase CCAAT-Binding Factor Schizosaccharomyces pombe Schizosaccharomyces pombe Proteins Cyclin-dependent kinase 7 Research Article Transcription Factors |
Popis: | 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. pombe HAP2) was obtained by functional complementation in an S. cerevisiae hap2 mutant and retains the ability to associate with HAP3 and HAP4. We have previously demonstrated that the HAP2 subunit of the CCAAT-binding transcriptional activation complex from S. cerevisiae contains a 65-amino-acid "essential core" structure that is divisible into subunit association and DNA recognition domains. Here we show that Php2 contains a 60-amino-acid block that is 82% identical to this core. The remainder of the 334-amino-acid protein is completely without homology to HAP2. The function of php2 in S. pombe was investigated by disrupting the gene. Strikingly, like HAP2 in S. cerevisiae, the S. pombe gene is specifically involved in mitochondrial function. This contrasts to the situation in mammals, in which the homologous CCAAT-binding complex is a global transcriptional activator. |
Databáze: | OpenAIRE |
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