Date of Award:
5-2021
Document Type:
Thesis
Degree Name:
Master of Science (MS)
Department:
Chemistry and Biochemistry
Committee Chair(s)
Joan M. Hevel
Committee
Joan M. Hevel
Committee
Sean J. Johnson
Committee
Nicholas E. Dickenson
Abstract
If you imagined a living cell as a factory, enzymes would be the workers with each individually performing a very specific and important job. If a job is not done correctly it could be detrimental to the performance of assembly lines and devastate a businesses’ existence. For enzymes, their jobs occur on a biological level by catalyzing reactions inside the cell, which can include altering another protein and the pathway it is involved in. Protein arginine methyltransferases, or PRMTs, is an example of an enzyme that modifies protein substrates. It does this by adding one or two methyl groups onto an arginine within a target proteins structure, which can alter the proteins function in a cell. This may include turning the substrate protein’s activity on or off, preventing or increasing interactions with other proteins, or altering the protein’s location in the cell.
Methylation performed by PRMTs in a cell influences critical cell processes such as DNA repair, transcriptional regulation, and RNA processing. Since PRMTs are integrated in many cell functions, it is not surprising that the malfunction of this enzyme can cause health issues such as cardiovascular disease and cancer. This means PRMTs are a suitable therapeutic target for treating diseased states, however further investigation of their mechanisms of function is required.
Checksum
6597d28e9c30124fe09be8a09b483436
Recommended Citation
Ortolano, Ariana N., "Characterizing Oligomeric State Changes of Protein Arginine Methyltransferase 1 as a Mechanism for Regulating Activity" (2021). All Graduate Theses and Dissertations, Spring 1920 to Summer 2023. 8054.
https://digitalcommons.usu.edu/etd/8054
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