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Researchers Uncover Previously Unstudied Cancer Enzyme
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Researchers Uncover Previously Unstudied Cancer Enzyme

Researchers Uncover Previously Unstudied Cancer Enzyme
News

Researchers Uncover Previously Unstudied Cancer Enzyme

State-of-the-Art Mass Spectrometry is used a lot in protein research Credit: Simon Skipper
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Researchers do not know how all the proteins and enzymes in the human body function, far from it. Now researchers at the University of Copenhagen have come a bit closer to understanding how an enzyme that appears to be important to cancer development behaves inside the cells. 


The new study that has just been published in the scientific journal Nature Communications shows first of all that the enzyme METTL13 helps control the formation of new proteins in the cells.


‘Mistakes in the production of proteins are undesirable, as we know from other studies that it can result in the development of cancer tumours and degenerative brain disorders like Alzheimer’s and Parkinson’s. Therefore, the new knowledge of how this enzyme functions is significant’, says Professor Jesper Velgaard Olsen from the Novo Nordisk Foundation Center for Protein Research.


The enzyme helps control protein synthesis by placing so-called methyl marks on a particular protein called eEF1A.


’If methyl is not attached correctly to the protein it will not be able to do its job properly. And that again affects the formation of proteins in the cell, which will take place at a suboptimal pace, and even though that may not sound so bad, it appears to be connected with very serious disorders’, says Postdoc Magnus Jakobsson from the Novo Nordisk Foundation Center for Protein Research.


The researchers have shown how the enzyme functions by studying isolated human cancer cells using advanced mass spectrometers which, in short, are able to identify and quantify proteins and their methyl-modifications in a cell.


Now the researchers hope the study will lead to the development of methods and drugs able to target and assure the enzyme to function as intended in our cells.

This article has been republished from materials provided by University of Copenhagen. Note: material may have been edited for length and content. For further information, please contact the cited source.

Reference: Jakobsson, M. E., Małecki, J. M., Halabelian, L., Nilges, B. S., Pinto, R., Kudithipudi, S., … Falnes, P. Ø. (2018). The dual methyltransferase METTL13 targets N terminus and Lys55 of eEF1A and modulates codon-specific translation rates. Nature Communications, 9(1), 3411. https://doi.org/10.1038/s41467-018-05646-y

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