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Cornell researchers discover new protein modification patterns in C. elegans, a type of roundworm.

March 13, 2024

Cornell Researchers Discover New Protein Modification Patterns in C. Elegans

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A new study on fatty acid acylation, or attachment, patterns onto proteins in Caenorhabditis elegans, a type of roundworm, provides a foundation for future discoveries around protein function and its association with various diseases.

The study, published by Prof. Frank Schroeder, chemistry and chemical biology, on Jan. 22, found new protein modification patterns in C. elegans through multiple techniques.

Fatty acid acylation is a process that adds branched fatty acid chains to proteins. These modifications enable proteins to anchor onto cell membranes, and may also serve various functions based on which fatty acids are added to the protein. 

According to study co-author Bingsen Zhang grad the team utilized two techniques — high-resolution mass spectroscopy and click chemistry — to identify the modified proteins and fatty acid chains involved in the process.

Using click chemistry, the researchers developed a probe to detect proteins by incorporating them into fatty acid modifications. They used mass spectroscopy, which ionizes molecules and puts them through an electrical current in order to observe their deflection and map them on a spectrum, to identify and determine the molecular weights of both modified proteins and attached fatty acid chains.

The team selected C. elegans as a model organism because it has various biological similarities to humans, including fatty acid acylation of proteins. Model organisms are species commonly used in fundamental biology research. 

“People use [C. elegans] because there are many conserved gene pathways and fundamental biological processes in humans,” Zhang said. 

The researchers discovered that fatty acid acylation is specific, as fatty acids are added to certain amino acids, such as lysine, cysteine, glycine and serine, that make up these proteins. They also found that the fatty acids attached to these amino acids differ as well, particularly in the structure and amount of carbons in each fatty acid. 

The diversity of fatty acid modifications indicates a link between the synthesis of various fatty acids and protein function. By understanding this connection, researchers can investigate how fatty acid acylation of proteins can potentially influence various health conditions, such as cancer, neurodegeneration, cardiovascular disorders and infectious diseases.

Fatty acid acylation can also be further linked to diet and the gut microbiome. Some fatty acids involved in protein modification, such as 15-methylhexadecanoic acid, are typically synthesized by C. elegans — however, in mammals, they can be absorbed from food intake or produced by microbes in the gut.

Zhang explained this research opens opportunities to understand how fatty acids affect the function of modified proteins.

“We present the first comprehensive resource on proteins in C. elegans modified by fatty acids,” Zhang said. “People can start from here to study the function of protein fatty acid acylation. For us, we may further look at how these branched chain fatty acids are incorporated into proteins.”

Kaitlyn Lee can be reached at [email protected].