Phototriggered protein syntheses by using (7-diethylaminocoumarin-4-yl)methoxycarbonyl-caged aminoacyl tRNAs
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Locking a major component of protein synthesis in a molecular cage that can be rapidly opened by a laser beam can control when and where proteins are made.
The time and location of protein generation determines a cell’s biological function. Previous efforts to control this process using light have produced poorly functioning proteins because key components were overexposed to UV radiation.
A team of researchers from Okayama University used the molecular compound (7-diethylaminocoumarin-4-yl) methoxycarbonyl (DEACM) as a cage to trap aa-tRNA, an essential molecule in protein synthesis. They applied a laser beam to the DEACM cage which broke up in just 20 seconds and released the aa-tRNA into the cell where it could start building proteins. The team used this technique to spatially and temporally control protein synthesis in cultured cells, liposomes, a gel and mammal cells.
This method offers a promising tool for investigating how cell function is affected by the time and site of protein synthesis, the authors say.
- Nature Communications 7,12507 (2016). doi: 10.1038/ncomms12501
|Okayama University, Japan||1.00|