Rapid regulation of protein activity in fission yeast

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• 作者：Cathrine A B?e (1)
  Ignacio Garcia (3)
  Chen-Chun Pai (2)
  Jeffrey R Sharom (4)
  Henriette C Skj?lberg (1)
  Erik Boye (1)
  Stephen Kearsey (2)
  Stuart A MacNeill (3)
  Michael D Tyers (4)
  Beáta Grallert (1)
  
• 刊名：BMC Cell Biology
• 出版年：2008
• 出版时间：December 2008
• 年：2008
• 卷：9
• 期：1
• 全文大小：1073KB
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• 作者单位：Cathrine A B?e (1)
  Ignacio Garcia (3)
  Chen-Chun Pai (2)
  Jeffrey R Sharom (4)
  Henriette C Skj?lberg (1)
  Erik Boye (1)
  Stephen Kearsey (2)
  Stuart A MacNeill (3)
  Michael D Tyers (4)
  Beáta Grallert (1)
  
  1. Department of Cell Biology, Rikshospitalet-Radiumhospitalet Medical Centre, Montebello, 0310 Oslo, Norway
  3. Department of Molecular Biology, University of Copenhagen, K?benhavns Biocenter, Ole Maal?es Vej 5, 2200, Copenhagen N, Denmark
  2. Department of Zoology, University of Oxford, South Parks Road, Oxford, OX1 3PS, UK
  4. Samuel Lunenfeld Research Institute, Room 1080, Mount Sinai Hospital, 600 University Avenue, Toronto Ontario, M5G 1X5, Canada
  

文摘

Background The fission yeast Schizosaccharomyces pombe is widely-used as a model organism for the study of a broad range of eukaryotic cellular processes such as cell cycle, genome stability and cell morphology. Despite the availability of extensive set of genetic, molecular biological, biochemical and cell biological tools for analysis of protein function in fission yeast, studies are often hampered by the lack of an effective method allowing for the rapid regulation of protein level or protein activity. Results In order to be able to regulate protein function, we have made use of a previous finding that the hormone binding domain of steroid receptors can be used as a regulatory cassette to subject the activity of heterologous proteins to hormonal regulation. The approach is based on fusing the protein of interest to the hormone binding domain (HBD) of the estrogen receptor (ER). The HBD tag will attract the Hsp90 complex, which can render the fusion protein inactive. Upon addition of estradiol the protein is quickly released from the Hsp90 complex and thereby activated. We have tagged and characterised the induction of activity of four different HBD-tagged proteins. Here we show that the tag provided the means to effectively regulate the activity of two of these proteins. Conclusion The estradiol-regulatable hormone binding domain provides a means to regulate the function of some, though not all, fission yeast proteins. This system may result in very quick and reversible activation of the protein of interest. Therefore it will be a powerful tool and it will open experimental approaches in fission yeast that have previously not been possible. Since fission yeast is a widely-used model organism, this will be valuable in many areas of research.