A new study delves into the microscopic universe of proteins, unveiling an aspect of their existence that could hold profound implications for the understanding and treatment of a myriad of human diseases.
Through meticulous investigation using high-resolution mass spectrometry, researchers discovered critical patterns of fatty acid attachment in the model organism C. elegans, a microscopic worm that offers a window into fundamental biological processes. The study, “Amino acid and protein specificity of protein fatty acylation in C. elegans,” published Jan. 22 in PNAS.
Imagine proteins as tiny engines driving the machinery of life. Just as engines require modifications to optimize performance, proteins undergo ‘protein modification’ – a crucial process altering their function, location, and lifespan. A key player in this modification process is protein fatty acid attachment (‘protein fatty acylation’), akin to adding a specialized component (i.e., fatty acids) that allows proteins to anchor themselves to cellular membranes.
“We were surprised to discover that different amino acids are modified with fatty acids from distinct biosynthetic pathways,” said senior author Frank Schroeder, professor of chemistry and chemical biology in the College of Arts and Sciences and a professor at the Boyce Thompson Institute. “This unexpected finding highlights the link between protein modification and specific fat metabolic pathways. It also serves as a foundation for further research into how protein function is affected by different fatty acids and their metabolism.”