Characterization of Caenorhabditis elegans PRMT1.
Class
Article
College
College of Science
Faculty Mentor
Joan Hevel
Presentation Type
Poster Presentation
Abstract
Protein arginine methyltransferases (PRMTs) are a family of enzymes which help to mediate a number of important cellular processes, including the cell cycle and chromatin remodeling. Perhaps unsurprisingly, misregulation of the enzymes in the PRMT family has been liked to several serious human diseases including heart disease and cancer. These enzymes modify other proteins by the addition of a small chemical group and this modification serves as a marker to initiate downstream processes. Despite the apparent importance of these enzymes in cellular function and dysfunction, relatively little is known about the processes that ultimately regulate the PRMT enzymes. Previously, we determined that oxidants and antioxidants can alter the activity of Rattus norvegicus PRMT1, this opens the possibility that the cellular oxidative balance could serve as a regulatory mechanism for the PRMTs in cells. An ideal approach to testing this hypothesis would involve the use of transgenic organisms lacking functional PRMT1, and observing how these organisms respond to oxidative stress. However in many of the organisms previously tested loss of functional PRMT1 is a lethal mutation. Recently Caenorhabditis elegans, were identified as organism which can survive PRMT1 knockout, and thus are an ideal model system for PRMT1 studies. However in our work with R. norvegicus PRMT1 we identified the chemical components, called cysteine residues, which are responsible for oxidative switching and these components are not present in C. elegans PRMT1. It is unclear if the C. elegans version of the enzyme has an oxidative switch. We have cloned and purified active C. elegans PRMT1 and we will work characterize the oxidative behavior of this enzyme.
Location
The North Atrium
Start Date
4-12-2018 10:30 AM
End Date
4-12-2018 11:45 AM
Characterization of Caenorhabditis elegans PRMT1.
The North Atrium
Protein arginine methyltransferases (PRMTs) are a family of enzymes which help to mediate a number of important cellular processes, including the cell cycle and chromatin remodeling. Perhaps unsurprisingly, misregulation of the enzymes in the PRMT family has been liked to several serious human diseases including heart disease and cancer. These enzymes modify other proteins by the addition of a small chemical group and this modification serves as a marker to initiate downstream processes. Despite the apparent importance of these enzymes in cellular function and dysfunction, relatively little is known about the processes that ultimately regulate the PRMT enzymes. Previously, we determined that oxidants and antioxidants can alter the activity of Rattus norvegicus PRMT1, this opens the possibility that the cellular oxidative balance could serve as a regulatory mechanism for the PRMTs in cells. An ideal approach to testing this hypothesis would involve the use of transgenic organisms lacking functional PRMT1, and observing how these organisms respond to oxidative stress. However in many of the organisms previously tested loss of functional PRMT1 is a lethal mutation. Recently Caenorhabditis elegans, were identified as organism which can survive PRMT1 knockout, and thus are an ideal model system for PRMT1 studies. However in our work with R. norvegicus PRMT1 we identified the chemical components, called cysteine residues, which are responsible for oxidative switching and these components are not present in C. elegans PRMT1. It is unclear if the C. elegans version of the enzyme has an oxidative switch. We have cloned and purified active C. elegans PRMT1 and we will work characterize the oxidative behavior of this enzyme.