ArticleBMC cell biology2008
Rapid regulation of protein activity in fission yeast.
Article in BMC cell biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- A Tetracycline-Inducible Promoter Replacement System formicroPublication biology · 2025Article
- Rapid depletion of target proteins in plants by an inducible protein degradation system.The Plant cell · 2024Article
- The longevity and reversibility of quiescence inCell cycle (Georgetown, Tex.) · 2023Article
- Cosegregation of asymmetric features during cell division.Open biology · 2021Article
- Functional Improvement of Human Cardiotrophin 1 Produced in Tobacco Chloroplasts by Co-expression with Plastid Thioredoxin m.Plants (Basel, Switzerland) · 2020Article
- Rapid regulation of nuclear proteins by rapamycin-induced translocation in fission yeast.Yeast (Chichester, England) · 2014Article
- GINS inactivation phenotypes reveal two pathways for chromatin association of replicative alpha and epsilon DNA polymerases in fission yeast.Molecular biology of the cell · 2009Article
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Authors and funding
10 authors.
Funding
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Abstract
backgroundThe 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.
resultsIn 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.
conclusionThe 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.
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