February 2022 Kentucky Lake Section Meeting

Protein Arginine methyltransferases:
an investigation of structural factors that control activity and product specificity.

Featuring Dr. Betsy Caceres
Assistant Professor, Union University

Thursday, February 24th 

Dinner @ 6:00 pm
Presentation @ 7:00 pm
at Fresh Market Restaurant
2255 E. Wood St
Paris, TN 38242

Dinner Price is $10 (Students $5)

Abstract:  Protein arginine methylation is an essential post-translational modification involved in many important biological processes. Some examples are transcription, RNA splicing, signal transduction, DNA repair, viral replication, and chromatin remodeling. In recent years, the significance of protein arginine methyltransferases (PRMTs) in human diseases has been increasingly studied, especially in cardiovascular disease and cancer. Although the importance of this enzyme is recognized, the understanding of the fundamental biochemistry of PRMTs is still limited. Very little information is available to explain how or why any of the PRMT isoforms target their cognate protein substrates, and more so, what determines which arginine within a protein substrate should be methylated. One of the great challenges when studying this family of proteins arises from the fact that different methylation statuses (monomethyl arginine [MMA], asymmetric dimethyl [ADMA], or symmetric dimethyl [SDMA]) of the same substrate can lead to distinct biological outputs. Therefore, to understand how this family of proteins functions and how to control them, it’s essential to understand how product specificity is achieved. In order to better understand the product specificity and activity of this family of enzymes, two Protein arginine methyltransferases that are responsible for two different methylation statuses have been used as models in our studies; PRMT1, which is responsible for ADMA and MMA formation, and TbPRMT7, which can only form MMA. Using the crystal structure of these enzymes and the available knowledge of PRMT activity regulation as a guide, we have found that there are several factors both structural and external that contribute to controlling the specific PRMT product formation and overall activity. This knowledge is crucial for the design of new drugs that would help us target these proteins in the diseases they are involved in.

Bio: Dr. Caceres graduated with a bachelor’s in pharmacy from Central East University in the Dominican Republic. She was awarded a presidential scholarship for her master’s in Biochemistry and later another one for her Ph.D. in Biochemistry at Utah State University. Dr. Caceres’s Ph.D. work was focused on Protein Arginine Methyltransferases and she has several publications from this work. After graduating, Ishe worked for a year in an X-ray crystallography lab at Utah State University where she reconstituted the yeast exosome. Currently, she serves as an assistant professor of Biochemistry in the Chemistry department at Union University where she is also a co-advisor to the Union University Student Members of the American Chemical Society (SMACS) chapter.

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