Identification of Trm7 residues required for Trm734 binding for tRNA methyltransferase activity in yeast

Simple item record
dc.contributor.authorLe, Thao Linh (Rosie)
dc.contributor.authorFraley, Morgan E.
dc.contributor.authorLe, Linh
dc.contributor.authorMullins, Alex K.
dc.contributor.authorFunk, Holly M.
dc.contributor.authorBekele, Bereket T.
dc.contributor.authorGuy, Adrian R.
dc.contributor.authorGuy, Michael P.
dc.date.accessioned2021-11-11T19:16:58Z
dc.date.available2021-11-11T19:16:58Z
dc.date.created2021
dc.description2021 Celebration of Student Research and Creativity presentationen_US
dc.description.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."en_US
dc.description.urihttps://youtu.be/CMetQ_JPkLEen_US
dc.identifier.urihttp://hdl.handle.net/11216/4143
dc.language.isoen_USen_US
dc.publisherNorthern Kentucky Universityen_US
dc.relation.ispartofseriesCelebration of Student Research and Creativity;2021
dc.subjectTransfer RNAen_US
dc.subjectCells Growthen_US
dc.subjectIntellectual disabilityen_US
dc.titleIdentification of Trm7 residues required for Trm734 binding for tRNA methyltransferase activity in yeasten_US
dc.typePresentationen_US

Files

Collections

Student Research and Creativity