PUBLICATION
General Method for Regulating Protein Stability with Light
- Authors
- Bonger, K.M., Rakhit, R., Payumo, A.Y., Chen, J.K., and Wandless, T.J.
- ID
- ZDB-PUB-131202-9
- Date
- 2014
- Source
- ACS Chemical Biology 9(1): 111-5 (Journal)
- Registered Authors
- Chen, James K.
- Keywords
- none
- MeSH Terms
-
- Animals
- Avena/chemistry
- Avena/genetics*
- Light
- Luminescent Proteins/chemistry*
- Luminescent Proteins/genetics*
- Mice
- NIH 3T3 Cells
- Photolysis*
- Phototropins/chemistry*
- Phototropins/genetics*
- Protein Engineering
- Protein Stability*
- Protein Structure, Tertiary
- Recombinant Fusion Proteins/chemistry
- Recombinant Fusion Proteins/genetics
- Zebrafish
- PubMed
- 24180414 Full text @ ACS Chem. Biol.
Citation
Bonger, K.M., Rakhit, R., Payumo, A.Y., Chen, J.K., and Wandless, T.J. (2014) General Method for Regulating Protein Stability with Light. ACS Chemical Biology. 9(1):111-5.
Abstract
Post-translational regulation of protein abundance in cells is a powerful tool for studying protein function. Here, we describe a novel genetically encoded protein domain that is degraded upon exposure to nontoxic blue light. We demonstrate that fusion proteins containing this domain are rapidly degraded in cultured cells and in zebrafish upon illumination.
Genes / Markers
Expression
Phenotype
Mutations / Transgenics
Human Disease / Model
Sequence Targeting Reagents
Fish
Orthology
Engineered Foreign Genes
Mapping