Phototriggered protein syntheses by using (7-diethylaminocoumarin-4-yl)methoxycarbonyl-caged aminoacyl tRNAs

Journal: Nature Communications

Published: 2016-08-17

DOI: 10.1038/ncomms12501

Affiliations: 1

Authors: 6

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Research Highlight

Protein production with laser precision

© Paper Boat Creative/DigitalVision/Getty

© Paper Boat Creative/DigitalVision/Getty

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.

Supported content

  1. Nature Communications 7,12507 (2016). doi: 10.1038/ncomms12501
Institutions FC WFC
Division of Medical Bioengineering, Okayama University, Japan 1 1

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