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  Efficient protein depletion by genetically controlled deprotection of a dormant N-degron

Taxis, C., Stier, G., Spadaccini, R., & Knop, M. (2009). Efficient protein depletion by genetically controlled deprotection of a dormant N-degron. Molecular Systems Biology, 5: 267, pp. 1-7. doi:10.1038/msb.2009.25.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-4EE6-0 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002C-4EE7-E
Genre: Journal Article
Alternative Title : Efficient protein depletion by genetically controlled deprotection of a dormant N-degron

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 Creators:
Taxis, Christof, Author
Stier, Gunter1, Author              
Spadaccini, Roberta, Author
Knop, Michael, Author
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1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              

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Free keywords: development, protein inactivation, regulated protein inactivation, tissue-specific
 Abstract: Methods that allow for the manipulation of genes or their products have been highly fruitful for biomedical research. Here, we describe a method that allows the control of protein abundance by a genetically encoded regulatory system. We developed a dormant N−degron that can be attached to the N−terminus of a protein of interest. Upon expression of a site−specific protease, the dormant N−degron becomes deprotected. The N−degron then targets itself and the attached protein for rapid proteasomal degradation through the N−end rule pathway. We use an optimized tobacco etch virus (TEV) protease variant combined with selective target binding to achieve complete and rapid deprotection of the N−degron−tagged proteins. This method, termed TEV protease induced protein inactivation (TIPI) of TIPI−degron (TDeg) modified target proteins is fast, reversible, and applicable to a broad range of proteins. TIPI of yeast proteins essential for vegetative growth causes phenotypes that are close to deletion mutants. The features of the TIPI system make it a versatile tool to study protein function in eukaryotes and to create new modules for synthetic or systems biology

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Language(s): eng - English
 Dates: 2009-01-232009-03-172009-04-282009-04-28
 Publication Status: Published in print
 Pages: 7
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Degree: -

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Title: Molecular Systems Biology
Source Genre: Journal
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Publ. Info: London : Nature Pub. Group
Pages: - Volume / Issue: 5 Sequence Number: 267 Start / End Page: 1 - 7 Identifier: ISSN: 1744-4292
CoNE: https://pure.mpg.de/cone/journals/resource/1000000000021290