Identification of Trm7 residues required for Trm734 binding for tRNA methyltransferase activity in yeast
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Northern Kentucky University
Abstract
"Post-transcriptional modifications are made on tRNA, an important molecule for the synthesis of proteins, that allow for functional proteins and cell growth. The enzymes that are involved in the modification process are still being identified in higher eukaryotes, including humans. In yeast, it has been shown that Trm7 forms a complex with Trm732 and Trm734 to modify tRNA at positions 32 and 34, respectively. In humans, the lack of Trm7 causes intellectual disability. The crystal structure of the Trm7- Trm734 complex has been solved, however, the Trm7 residues that are important for the interaction for these proteins are still being investigated. We have identified Trm7 Y138 as important for binding to Trm734 using site-directed mutagenesis and a spot test assay. We are now testing another 10 residues that are predicted to be important for binding based on the crystal structure. Understanding this interaction can be used to identify Trm7 residues important for the Trm7- Trm732 interaction, whose structure has yet to be solved."
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2021 Celebration of Student Research and Creativity presentation
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Presentation
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Keywords
Transfer RNA, Cells Growth, Intellectual disability