Messenger RNA (mRNA) is a molecule composed of nucleic acids that transfers the genetic information contained in DNA to produce the proteins that ensure the correct biological operation of every type of cell.  In this activity, mRNA is supported by other proteins including those known as chaperones, stress proteins, or Heat Shock Proteins (HSP).

A new study, coordinated by Gian Gaetano Tartaglia from the “Charles Darwin” Department of Biology and Biotechnology, in collaboration with the Barcelona Centre for Genomic Regulation and the University of Frankfurt has revealed for the first time that, under certain circumstances, messenger RNA could act as a molecular chaperone, blocking the formation of protein aggregates that are potentially toxic to our organisms. The results of the study have been published on Nature Communications.

In particular, researchers observed the Heat Shock Proteins 70 kilodaltons chaperone which, interacting with many proteins, is considered an ideal candidate to study the effects of protein aggregation.

As per their predictions, the researchers experimentally demonstrated for the first time that, under conditions of stress, messenger RNA HSP70 behaves as its final protein product: it has the ability to promote the removal of the protein aggregates that are responsible for serious neuro-degenerative diseases such as Alzheimer’s and Amyotrophic Lateral Sclerosis.

“In our study,” explains Prof. Tartaglia, “we observed that the quantity of structure in RNA molecules is correlated to the number of protein interactions. This reveals the existence of a regulation level that directly associates RNA to its protein products for all genes that are highly active in cellular processes.”

The results of the study extend our knowledge about the mechanisms through which protein aggregates are removed and recognize the fundamental role in this played by RNA, which controls more cellular processes than previously thought and that may play a fundamental role in neuro-degenerative pathologies.

References:

RNA structure drives interaction with proteins - de Groot, N. S., Armaos, A., Graña-Montes, R., Alriquet, M., Calloni, G., Vabulas, R. M., & Tartaglia, G. G. - Nature Communications 2019, 10, 3246. DOI: 10.1038/s41467-019-10923-5

Further Information

Gian Gaetano Tartaglia
“Charles Darwin” Department of Biology and Biotechnology, Sapienza University of Rome
giangaetano.tartaglia@uniroma1.it