(ORDO NEWS) — In the process of life, cells are constantly activating many genes and protein pathways, and now people have been able to make them “record” the history of these events in the form of a long protein chain, which can later be “read”.
To assess the response of living cells to various events – for example, the impact of a drug – requires monitoring microscopic changes in their physiology associated with the production of new proteins or the expression of new genes.
Since tracking them in real time – say, using fluorescent markers – is quite difficult, researchers from the Massachusetts Institute of Technology (USA) made mouse brain cells “keep a record” of events occurring in them.
Naturally, such a record is made not with the help of paper and ink, but with the help of a special self-assembling protein, to which new blocks are added at certain cellular events.
Later, such a protein can be extracted from the cell, marked and examined under a microscope, which will allow us to accurately reconstruct the chronological chain.
To provide a “chronicle”, scientists forced a living cell to produce protein subunits that have the ability to self-assemble.
One of these subunits was produced all the time, while the other was produced only at the right events in the cell, such as the activation of a particular gene.
In other words, most of the “memory protein” was made up of ordinary subunits, to which fluorescent labels of the same color were bound.
But if a dot of a different color appeared in the chain, then the desired gene was activated at that moment.
So far, the technique has only been tested on one particular gene, c-fos , in cultured mouse brain cells and in live mice.
However, theoretically, this method can be applied to almost any gene or protein in any cell of any living organism.
The only limitation is the size of the record: some cells are too small to fit a long protein chain without harming themselves.
However, this limitation can also be circumvented by reducing the “temporal resolution” and slowing down the synthesis of protein units.
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