Expression of the SV40 promoter in fission yeast: Identification and characterization of an AP-1-like factor

• Published in: Cell Vol. 53; no. 4; pp. 659 - 667
• Main Authors: Jones, Robert H., Moreno, Sergio, Nurse, Paul, Jones, Nicholas C.
• Format: Journal Article
• Language: English
• Published: Cambridge, MA Elsevier Inc 20.05.1988; Cell Press
• Subjects: Biological and medical sciences; Biotechnology; Deoxyribonuclease I; Fundamental and applied biological sciences. Psychology; Gene Expression Regulation; Genetic engineering; Genetic technics; HeLa Cells; Humans; Methods. Procedures. Technologies; Phosphoric Monoester Hydrolases - metabolism; Phosphorylation; Plasmids; Promoter Regions, Genetic; Proto-Oncogene Proteins c-jun - genetics; Saccharomyces cerevisiae - genetics; Saccharomycetales - genetics; Schizosaccharomyces - genetics; Simian virus 40 - genetics; Transcription Factors - genetics; Transcription, Genetic; Yeast; Transcription; Transcription promoter; Polyomavirus; Papovaviridae; Gene expression; Fungi; Virus; Regulation(control); Enhancer sequence; Schizosaccharomyces pombe; Ascomycetes; Transcription factor; SV40 virus; Thallophyta
• ISSN: 0092-8674; 1097-4172
• DOI: 10.1016/0092-8674(88)90581-8

The SV40 promoter is expressed well in the fission yeast S. pombe, and it initiates transcription at the same site as in mammalian cells. The majority of the enhancer sequences, however, do not contribute to this activity. DNAase I footprint analysis of the promoter revealed the presence of an AP-1-like factor in S. pombe cells that protects a region of the promoter almost identical to that protected by human AP-1. The specificity of binding of the yeast and mammalian AP-1 proteins was found to be similar. We have found two AP-1-like binding activities in budding yeast cells, one of which appears quite distinct from the binding activity of the product of the budding yeast GCN4 gene. We also demonstrate that in fission yeast the AP-1 binding site can act as an upstream activating sequence. The DNA-protein complexes containing the mammalian AP-1 and fission yeast AP-1-like factors are sensitive to phosphatase treatment, indicating that they may be phosphorylated.