Discovery of the binding of highly specific fatty acids to proteins

Discovery of the binding of highly specific fatty acids to proteins

This article has been reviewed in accordance with Science

Fact check

Peer-reviewed publication

trusted source

Proofreading


Fluorescence imaging of C. elegans fed with a new chemical probe developed in this study – an analogue of branched-chain fatty acids. The red signal is derived from a selective “click chemistry” reaction between the probe and the red fluorescent dye. Credit: Schroder Laboratory/Boyce Thompson Institute

× Close


Fluorescence imaging of C. elegans fed with a new chemical probe developed in this study – an analogue of branched-chain fatty acids. The red signal is derived from a selective “click chemistry” reaction between the probe and the red fluorescent dye. Credit: Schroder Laboratory/Boyce Thompson Institute

In a world where the complexities of molecular biology seem as vast and mysterious as the universe, a new study delves into the microscopic universe of proteins, revealing a fascinating aspect of their existence. This discovery could have profound implications for the understanding and treatment of countless human diseases.

Imagine proteins as tiny engines that drive life’s machines. Just as engines need modifications to optimize performance, proteins undergo “protein modification” – a crucial process that changes their function, location and lifespan. A key player in this modification process is the attachment of fatty acids to protein (“lipoprotein acetylation”), which is analogous to the addition of a specialized component (i.e. fatty acid) that allows proteins to attach themselves to cellular membranes.

Through careful investigation using high-resolution mass spectrometry, scientists from the Boyce Thompson Institute (BTI) have discovered critical patterns of fatty acid binding in the model organism C. elegans, a microscopic worm that provides a window into fundamental biological processes.

By harnessing the power of “click chemistry” – a technique celebrated and awarded two Nobel Prizes in Chemistry – the researchers have succeeded in mapping how different amino acids in proteins are specifically modified with different fatty acids. Their work is published in the journal Proceedings of the National Academy of Sciences.

“We were surprised to find that different amino acids are modified with fatty acids from distinct biosynthetic pathways,” wrote Frank Schroeder, a professor at BTI and senior author of the study. “This unexpected finding highlights the relationship between protein modification and specific lipid metabolic pathways. It also serves as a basis for further research into how protein function is affected by different fatty acids and their metabolism.”

The study, titled “Amino acid and protein specificity of protein fatty acyls in C. elegans,” is not just about understanding the inner workings of a tiny worm. The implications are wide-ranging and highly relevant to human health. The binding of fatty acids to protein is a critical factor in diseases ranging from cancer to neurodegeneration, cardiovascular disorders, and even infectious diseases.

“What we learn from C. elegans contributes greatly to our basic understanding of this type of protein modification,” said Bingsen Zhang, a graduate student in Schroeder’s lab and first author of the study. “The more we understand about protein modification and function, the better we understand its central role in human health and disease.”

Furthermore, the study reveals the first example of extensive protein modification using branched-chain fatty acids, a discovery that may have parallels in higher animals and humans, given their presence in our diet and production by gut microbes. The relationship between diet, gut health, and protein modification could open new horizons in nutritional science.

Ultimately, this study is about the basic processes that keep every creature alive, from microscopic worms to humans. So, next time you see a worm, give a nod to the unlikely hero of biology and the scientists who are discovering its secrets. Because sometimes, the key to life’s biggest secrets lies in its smallest inhabitants.

more information:
Bingsen Zhang et al., Amino acid and protein specificity of lipoprotein acylation in C. elegans, Proceedings of the National Academy of Sciences (2024). doi: 10.1073/pnas.2307515121

Magazine information:
Proceedings of the National Academy of Sciences

You may also like...

Leave a Reply

Your email address will not be published. Required fields are marked *